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purification map7  (Addgene inc)


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    Addgene inc purification map7
    <t>MAP7</t> targets bidirectional cargoes to the microtubule plus-end by increasing the number of engaged kinesin motors. A, isolated phagosomes containing fluorescent beads were positioned on polarity-marked microtubules, and the forces were measured using an optical trap. These isolated phagosomes are transported by teams of kinesin-1, kinesin-2, and dynein motors (14). B, MAP7 binds in static patches (Fig. S1J; Movie S6), whereas tau forms both static and diffusive patches along the microtubule lattice (Fig. S1K). The mean dwell time of MAP7 is 114.5 ± 6.16 s (n = 221 events from 11 recordings, two independent experiments), compared with 14.9 ± 1.19 s for tau (n = 128 events from 26 recordings, two independent experiments). C, force traces were acquired at 2 kHz and median-filtered at 20 Hz. We observe force events directed toward both the minus-end (i, iii, and vii) and plus-end (ii, v, and vi) and also bidirectional force events (iv and viii) (0 nm: n = 689 events from 38 recordings, 11 independent experiments; 10 nm MAP7: n = 787 events from 40 recordings, 11 independent experiments). D, maximum forces for all trap displacements greater than 300 ms (top) and 500 ms (bottom) in duration were included in the histogram. Consistent with previous results (14, 30), plus-end–directed force events consist of unitary stall forces of kinesin-1 and kinesin-2, events where the motors detach before reaching their stall force, and rare events driven by multiple kinesins. Minus-end–directed forces indicate events driven by teams of several dynein motors (Fig. S1C). The frequency and magnitude of kinesin-driven forces increase in the presence of 10 nm MAP7. In response, dynein-mediated forces are reduced. The Bayesian information criterion was used to determine the optimal number of components to describe the force histograms (Fig. S1F). Mean forces for plus-end directed motors are 1.57, 2.38, and 4.5 and for minus-ended motors are 1.14, 1.6, 2.8, and 5.8 pN. With MAP7, mean forces of the multicomponent fits for plus-end–directed forces are 1.4, 2.4, 4.5, and 7.3 pN, and for minus-end–directed forces, they are 1.4, 2.7, and ≥9 pN (p < 0.001; Kolmogorov–Smirnov test; Fig. S5A). E, teams of kinesin and dynein motors remain engaged to the microtubule under load for longer durations in the presence of MAP7. The color of the trajectory indicates the duration of a stall event. The duration of force events is significantly longer for kinesin-driven events with MAP7 (<T0 nM,+> = 1.5 s, <T10 nM,+> = 2.5 s, p < 0.01), whereas the duration of dynein-driven forces is slightly decreased (<T0 nM,−> = 2.26 s, <T10 nM,−> = 1.8 s, p = not significant) (Fig. S5C). F, comparing the duration of events of similar maximum force indicates that MAP7 does not alter the duration of events driven by similar numbers of motors. G, the relative binding rate was calculated as the reciprocal of the dwell time (green periods) preceding a force event (yellow). H, MAP7 increases the relative binding rate of plus-ended motors on MAP7 decorated microtubules by 28% (<π0 nM,+> = 0.89 s−1, <π10 nM,+> = 1.14 s−1; <π0 nM,−> = 1.05 s−1, <π10 nM,−> = 1.15 s−1). Error bars, S.E.
    Purification Map7, supplied by Addgene inc, used in various techniques. Bioz Stars score: 90/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "MAP7 regulates organelle transport by recruiting kinesin-1 to microtubules"

    Article Title: MAP7 regulates organelle transport by recruiting kinesin-1 to microtubules

    Journal: The Journal of Biological Chemistry

    doi: 10.1074/jbc.RA119.008052

    MAP7 targets bidirectional cargoes to the microtubule plus-end by increasing the number of engaged kinesin motors. A, isolated phagosomes containing fluorescent beads were positioned on polarity-marked microtubules, and the forces were measured using an optical trap. These isolated phagosomes are transported by teams of kinesin-1, kinesin-2, and dynein motors (14). B, MAP7 binds in static patches (Fig. S1J; Movie S6), whereas tau forms both static and diffusive patches along the microtubule lattice (Fig. S1K). The mean dwell time of MAP7 is 114.5 ± 6.16 s (n = 221 events from 11 recordings, two independent experiments), compared with 14.9 ± 1.19 s for tau (n = 128 events from 26 recordings, two independent experiments). C, force traces were acquired at 2 kHz and median-filtered at 20 Hz. We observe force events directed toward both the minus-end (i, iii, and vii) and plus-end (ii, v, and vi) and also bidirectional force events (iv and viii) (0 nm: n = 689 events from 38 recordings, 11 independent experiments; 10 nm MAP7: n = 787 events from 40 recordings, 11 independent experiments). D, maximum forces for all trap displacements greater than 300 ms (top) and 500 ms (bottom) in duration were included in the histogram. Consistent with previous results (14, 30), plus-end–directed force events consist of unitary stall forces of kinesin-1 and kinesin-2, events where the motors detach before reaching their stall force, and rare events driven by multiple kinesins. Minus-end–directed forces indicate events driven by teams of several dynein motors (Fig. S1C). The frequency and magnitude of kinesin-driven forces increase in the presence of 10 nm MAP7. In response, dynein-mediated forces are reduced. The Bayesian information criterion was used to determine the optimal number of components to describe the force histograms (Fig. S1F). Mean forces for plus-end directed motors are 1.57, 2.38, and 4.5 and for minus-ended motors are 1.14, 1.6, 2.8, and 5.8 pN. With MAP7, mean forces of the multicomponent fits for plus-end–directed forces are 1.4, 2.4, 4.5, and 7.3 pN, and for minus-end–directed forces, they are 1.4, 2.7, and ≥9 pN (p < 0.001; Kolmogorov–Smirnov test; Fig. S5A). E, teams of kinesin and dynein motors remain engaged to the microtubule under load for longer durations in the presence of MAP7. The color of the trajectory indicates the duration of a stall event. The duration of force events is significantly longer for kinesin-driven events with MAP7 (<T0 nM,+> = 1.5 s, <T10 nM,+> = 2.5 s, p < 0.01), whereas the duration of dynein-driven forces is slightly decreased (<T0 nM,−> = 2.26 s, <T10 nM,−> = 1.8 s, p = not significant) (Fig. S5C). F, comparing the duration of events of similar maximum force indicates that MAP7 does not alter the duration of events driven by similar numbers of motors. G, the relative binding rate was calculated as the reciprocal of the dwell time (green periods) preceding a force event (yellow). H, MAP7 increases the relative binding rate of plus-ended motors on MAP7 decorated microtubules by 28% (<π0 nM,+> = 0.89 s−1, <π10 nM,+> = 1.14 s−1; <π0 nM,−> = 1.05 s−1, <π10 nM,−> = 1.15 s−1). Error bars, S.E.
    Figure Legend Snippet: MAP7 targets bidirectional cargoes to the microtubule plus-end by increasing the number of engaged kinesin motors. A, isolated phagosomes containing fluorescent beads were positioned on polarity-marked microtubules, and the forces were measured using an optical trap. These isolated phagosomes are transported by teams of kinesin-1, kinesin-2, and dynein motors (14). B, MAP7 binds in static patches (Fig. S1J; Movie S6), whereas tau forms both static and diffusive patches along the microtubule lattice (Fig. S1K). The mean dwell time of MAP7 is 114.5 ± 6.16 s (n = 221 events from 11 recordings, two independent experiments), compared with 14.9 ± 1.19 s for tau (n = 128 events from 26 recordings, two independent experiments). C, force traces were acquired at 2 kHz and median-filtered at 20 Hz. We observe force events directed toward both the minus-end (i, iii, and vii) and plus-end (ii, v, and vi) and also bidirectional force events (iv and viii) (0 nm: n = 689 events from 38 recordings, 11 independent experiments; 10 nm MAP7: n = 787 events from 40 recordings, 11 independent experiments). D, maximum forces for all trap displacements greater than 300 ms (top) and 500 ms (bottom) in duration were included in the histogram. Consistent with previous results (14, 30), plus-end–directed force events consist of unitary stall forces of kinesin-1 and kinesin-2, events where the motors detach before reaching their stall force, and rare events driven by multiple kinesins. Minus-end–directed forces indicate events driven by teams of several dynein motors (Fig. S1C). The frequency and magnitude of kinesin-driven forces increase in the presence of 10 nm MAP7. In response, dynein-mediated forces are reduced. The Bayesian information criterion was used to determine the optimal number of components to describe the force histograms (Fig. S1F). Mean forces for plus-end directed motors are 1.57, 2.38, and 4.5 and for minus-ended motors are 1.14, 1.6, 2.8, and 5.8 pN. With MAP7, mean forces of the multicomponent fits for plus-end–directed forces are 1.4, 2.4, 4.5, and 7.3 pN, and for minus-end–directed forces, they are 1.4, 2.7, and ≥9 pN (p < 0.001; Kolmogorov–Smirnov test; Fig. S5A). E, teams of kinesin and dynein motors remain engaged to the microtubule under load for longer durations in the presence of MAP7. The color of the trajectory indicates the duration of a stall event. The duration of force events is significantly longer for kinesin-driven events with MAP7 ( = 1.5 s, = 2.5 s, p < 0.01), whereas the duration of dynein-driven forces is slightly decreased ( = 2.26 s, = 1.8 s, p = not significant) (Fig. S5C). F, comparing the duration of events of similar maximum force indicates that MAP7 does not alter the duration of events driven by similar numbers of motors. G, the relative binding rate was calculated as the reciprocal of the dwell time (green periods) preceding a force event (yellow). H, MAP7 increases the relative binding rate of plus-ended motors on MAP7 decorated microtubules by 28% (<π0 nM,+> = 0.89 s−1, <π10 nM,+> = 1.14 s−1; <π0 nM,−> = 1.05 s−1, <π10 nM,−> = 1.15 s−1). Error bars, S.E.

    Techniques Used: Isolation, Binding Assay

    MAP7 recruits kinesin-1 to microtubules. A and B, MAP7 recruits full-length kinesin-1 to microtubules in a dose-dependent manner (see also Fig. S2B). MgADP-bound kinesin-1 is in a weakly bound state. Kinesin-1 hydrolyzes MgATP to drive processive movement. C, when present at high levels, MAP7 increases kinesin-1 run lengths by up to ∼30%, possibly due to rapid re-attachment (average run length: 0 nm = 2033 ± 493.8 nm; 5 nm = 1640 ± 463 nm; 10 nm = 1800 ± 937 nm; 25 nm = 2227 ± 411.2 nm; 75 nm = 3002 ± 265.5 nm). D, the frequency of both processive and diffusive motility of kinesin-1 increases to a similar degree with increasing MAP7 concentration (0 nm MAP7: n = 15 events, three recordings; 5 nm MAP7: n = 17 events from three recordings; 10 nm MAP7: n = 21 events from three recordings; 25 nm MAP7: n = 37 events from three recordings; 75 nm MAP7: n = 70 events from three recordings). E and F, beads transported by ∼1–2 kinesin-1 motors were positioned on the microtubule using a weak optical trap (k ∼0.004 pN/nm) and imaged as they moved along the microtubule. G, long, directed events toward the microtubule plus-end indicate motility by multiple kinesin-1 motors. H, teams of kinesin-1 motors are more processive on MAP7-decorated microtubule (I and J). The average run length of kinesin-1 motors with MAP7 increases by ∼8-fold (average run length (0 nm) = 595 ± 60 nm; average run length (10 nm) = 5320 ± 890 nm), whereas the velocity is unaffected (average velocity (0 nm) = 220 ± 16 nm/s; average velocity (10 nm) = 292 ± 45 nm/s) (0 nm: n = 72 events from 21 trajectories, two independent experiments; 10 nm MAP7: n = 32 events from 18 trajectories, two independent experiments). Error bars, S.E.
    Figure Legend Snippet: MAP7 recruits kinesin-1 to microtubules. A and B, MAP7 recruits full-length kinesin-1 to microtubules in a dose-dependent manner (see also Fig. S2B). MgADP-bound kinesin-1 is in a weakly bound state. Kinesin-1 hydrolyzes MgATP to drive processive movement. C, when present at high levels, MAP7 increases kinesin-1 run lengths by up to ∼30%, possibly due to rapid re-attachment (average run length: 0 nm = 2033 ± 493.8 nm; 5 nm = 1640 ± 463 nm; 10 nm = 1800 ± 937 nm; 25 nm = 2227 ± 411.2 nm; 75 nm = 3002 ± 265.5 nm). D, the frequency of both processive and diffusive motility of kinesin-1 increases to a similar degree with increasing MAP7 concentration (0 nm MAP7: n = 15 events, three recordings; 5 nm MAP7: n = 17 events from three recordings; 10 nm MAP7: n = 21 events from three recordings; 25 nm MAP7: n = 37 events from three recordings; 75 nm MAP7: n = 70 events from three recordings). E and F, beads transported by ∼1–2 kinesin-1 motors were positioned on the microtubule using a weak optical trap (k ∼0.004 pN/nm) and imaged as they moved along the microtubule. G, long, directed events toward the microtubule plus-end indicate motility by multiple kinesin-1 motors. H, teams of kinesin-1 motors are more processive on MAP7-decorated microtubule (I and J). The average run length of kinesin-1 motors with MAP7 increases by ∼8-fold (average run length (0 nm) = 595 ± 60 nm; average run length (10 nm) = 5320 ± 890 nm), whereas the velocity is unaffected (average velocity (0 nm) = 220 ± 16 nm/s; average velocity (10 nm) = 292 ± 45 nm/s) (0 nm: n = 72 events from 21 trajectories, two independent experiments; 10 nm MAP7: n = 32 events from 18 trajectories, two independent experiments). Error bars, S.E.

    Techniques Used: Concentration Assay

    MAP7 increases the forces generated by teams of kinesin-1. We measured forces by single kinesin-1 motors and teams at three motor densities (ratio of motors to beads in the conjugation reaction). A, 3300 kinesin-1s/bead resulted in motility driven by a single kinesin-1, where <50% of beads interacted with the microtubule; G, 6600 kinesin-1s/bead resulted in motility due to 1–2 engaged kinesin-1 motors; M, 13,000 kinesin-1s/bead resulted in 2–3 kinesin-1 motors. B and C, on beads driven by single kinesin-1 motors, force distributions indicate unitary stall force of kinesin-1 and substall detachment forces (mean forces of the multicomponent fits Fcomp = 1.3 and 4.03 pN). With the addition of MAP7, substall detachment events decrease, and the frequency of unitary stall force events due to single kinesin-1 increases (Fcomp = 4.23 and ≥9 pN) (p < 0.001; Kolmogorov–Smirnov test; Fig. S5B) (0 nm: n = 444 events from 25 recordings, four independent experiments; 10 nm MAP7: n = 536 events from 25 recordings, four independent experiments). H and I, on beads driven by ∼1–2 kinesin-1s, force distributions show three distinct populations: forces at unitary stall force of kinesin-1, detachment forces, and rare multimotor events (Fcomp = 1.27, 3.47, and 7 pN). With the addition of MAP7, detachment and low force events decrease, whereas the frequency of unitary stall force events increases (Fcomp = 1.17, 4, and 7 pN) (p < 0.001; Kolmogorov–Smirnov test; Fig. S5B). The frequency and magnitude of multimotor force events remain unchanged (0 nm: n = 479 events from 26 recordings, four independent experiments; 10 nm MAP7: n = 623 events from 24 recordings, four independent experiments). N and O, on beads driven by ∼2–3 kinesin-1 motors, force distribution shows three distinct populations: forces at unitary stall force of kinesin-1, low-force events, and multimotor events (Fcomp = 1.24, 3.64, and 7.5 pN). With MAP7, we observe a shift toward frequent high-force events driven by multiple engaged kinesin-1s (Fcomp = 4.24, 5.97, and 7.29) (p < 0.001; Kolmogorov–Smirnov test; Fig. S5B) (0 nm: n = 485 events from 23 recordings, three independent experiments; 10 nm MAP7: n = 378 events from 22 recordings, three independent experiments). D, J, P, and Fig. S3, the duration of stall events at a given force is not strongly influenced by MAP7, indicating that MAP7 does not affect the processivity of single kinesin motors. Single kinesin-1 motors (E) and teams of 1–2 kinesin-1 motors (K) bind much faster to MAP7-decorated microtubules. Q, the increase in binding rate is not observed for larger teams of 2–3 kinesin-1s, likely because attachment is no longer limited by the single-motor binding rate when many motors are available for binding (single kinesin-1: 0 nm = 0.77 s−1 and 10 nm = 0.95 s−1; teams of ∼1–2 kinesin-1s: 0 nm = 1.04 s−1 and 10 nm = 1.55 s−1; ∼2–3 kinesin-1s: 0 nm = 1.24 s−1 and 10 nm = 1.35 s−1). F, L, R, the force–velocity curves indicate that more kinesin-1 motors are simultaneously engaged when MAP7 is present, as indicated by higher velocities at the same load. Error bars, S.E.
    Figure Legend Snippet: MAP7 increases the forces generated by teams of kinesin-1. We measured forces by single kinesin-1 motors and teams at three motor densities (ratio of motors to beads in the conjugation reaction). A, 3300 kinesin-1s/bead resulted in motility driven by a single kinesin-1, where <50% of beads interacted with the microtubule; G, 6600 kinesin-1s/bead resulted in motility due to 1–2 engaged kinesin-1 motors; M, 13,000 kinesin-1s/bead resulted in 2–3 kinesin-1 motors. B and C, on beads driven by single kinesin-1 motors, force distributions indicate unitary stall force of kinesin-1 and substall detachment forces (mean forces of the multicomponent fits Fcomp = 1.3 and 4.03 pN). With the addition of MAP7, substall detachment events decrease, and the frequency of unitary stall force events due to single kinesin-1 increases (Fcomp = 4.23 and ≥9 pN) (p < 0.001; Kolmogorov–Smirnov test; Fig. S5B) (0 nm: n = 444 events from 25 recordings, four independent experiments; 10 nm MAP7: n = 536 events from 25 recordings, four independent experiments). H and I, on beads driven by ∼1–2 kinesin-1s, force distributions show three distinct populations: forces at unitary stall force of kinesin-1, detachment forces, and rare multimotor events (Fcomp = 1.27, 3.47, and 7 pN). With the addition of MAP7, detachment and low force events decrease, whereas the frequency of unitary stall force events increases (Fcomp = 1.17, 4, and 7 pN) (p < 0.001; Kolmogorov–Smirnov test; Fig. S5B). The frequency and magnitude of multimotor force events remain unchanged (0 nm: n = 479 events from 26 recordings, four independent experiments; 10 nm MAP7: n = 623 events from 24 recordings, four independent experiments). N and O, on beads driven by ∼2–3 kinesin-1 motors, force distribution shows three distinct populations: forces at unitary stall force of kinesin-1, low-force events, and multimotor events (Fcomp = 1.24, 3.64, and 7.5 pN). With MAP7, we observe a shift toward frequent high-force events driven by multiple engaged kinesin-1s (Fcomp = 4.24, 5.97, and 7.29) (p < 0.001; Kolmogorov–Smirnov test; Fig. S5B) (0 nm: n = 485 events from 23 recordings, three independent experiments; 10 nm MAP7: n = 378 events from 22 recordings, three independent experiments). D, J, P, and Fig. S3, the duration of stall events at a given force is not strongly influenced by MAP7, indicating that MAP7 does not affect the processivity of single kinesin motors. Single kinesin-1 motors (E) and teams of 1–2 kinesin-1 motors (K) bind much faster to MAP7-decorated microtubules. Q, the increase in binding rate is not observed for larger teams of 2–3 kinesin-1s, likely because attachment is no longer limited by the single-motor binding rate when many motors are available for binding (single kinesin-1: 0 nm = 0.77 s−1 and 10 nm = 0.95 s−1; teams of ∼1–2 kinesin-1s: 0 nm = 1.04 s−1 and 10 nm = 1.55 s−1; ∼2–3 kinesin-1s: 0 nm = 1.24 s−1 and 10 nm = 1.35 s−1). F, L, R, the force–velocity curves indicate that more kinesin-1 motors are simultaneously engaged when MAP7 is present, as indicated by higher velocities at the same load. Error bars, S.E.

    Techniques Used: Generated, Conjugation Assay, Binding Assay

    MAP7 directs transport toward the microtubule plus-end. A, we extended the mathematical model proposed by Muller et al. (40) to describe the interaction between teams of kinesin-1, kinesin-2, and dynein motors based on single-motor parameters including the motor stall force, detachment force, and unbinding and binding rates (14). We modeled the effect of MAP7 by increasing the binding rate of single kinesin-1 molecules by the same amount as we measured in optical trapping measurements. Kinesin-2 and dynein were assumed to be unaffected by MAP7. B, the increase in kinesin-1 binding rate biases simulated trajectories toward the plus-end (number of simulated trajectories, n = 100). C, we calculated run length as distance between reversals (29) and consider events >400 nm as processive. Plus-end–directed run lengths increase by ∼24%, whereas minus-end–directed run lengths decrease by ∼24%. D, the model results suggest that the shift in phagosome transport toward the microtubule plus-end that we observe can be described by simply increasing the kinesin-1 binding rate with no direct effect on kinesin-2 or dynein. E, the number of engaged kinesin and dynein motors changes in the presence of MAP7. A greater number of plus-ended motors are simultaneously engaged and exerting force, and as a result, minus-ended motors are under higher loads and are less processive. F, MAP7 and tau exhibit distinct localizations in neurons. Whereas MAP7 is enriched at axonal branches (21), tau is localized in a gradient along the axon. Thus, MAP7 might target cargoes to the microtubule plus-end at branch sites, whereas tau directs distal cargoes toward the cell body. Error bars, S.E.
    Figure Legend Snippet: MAP7 directs transport toward the microtubule plus-end. A, we extended the mathematical model proposed by Muller et al. (40) to describe the interaction between teams of kinesin-1, kinesin-2, and dynein motors based on single-motor parameters including the motor stall force, detachment force, and unbinding and binding rates (14). We modeled the effect of MAP7 by increasing the binding rate of single kinesin-1 molecules by the same amount as we measured in optical trapping measurements. Kinesin-2 and dynein were assumed to be unaffected by MAP7. B, the increase in kinesin-1 binding rate biases simulated trajectories toward the plus-end (number of simulated trajectories, n = 100). C, we calculated run length as distance between reversals (29) and consider events >400 nm as processive. Plus-end–directed run lengths increase by ∼24%, whereas minus-end–directed run lengths decrease by ∼24%. D, the model results suggest that the shift in phagosome transport toward the microtubule plus-end that we observe can be described by simply increasing the kinesin-1 binding rate with no direct effect on kinesin-2 or dynein. E, the number of engaged kinesin and dynein motors changes in the presence of MAP7. A greater number of plus-ended motors are simultaneously engaged and exerting force, and as a result, minus-ended motors are under higher loads and are less processive. F, MAP7 and tau exhibit distinct localizations in neurons. Whereas MAP7 is enriched at axonal branches (21), tau is localized in a gradient along the axon. Thus, MAP7 might target cargoes to the microtubule plus-end at branch sites, whereas tau directs distal cargoes toward the cell body. Error bars, S.E.

    Techniques Used: Binding Assay



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    <t>MAP7</t> targets bidirectional cargoes to the microtubule plus-end by increasing the number of engaged kinesin motors. A, isolated phagosomes containing fluorescent beads were positioned on polarity-marked microtubules, and the forces were measured using an optical trap. These isolated phagosomes are transported by teams of kinesin-1, kinesin-2, and dynein motors (14). B, MAP7 binds in static patches (Fig. S1J; Movie S6), whereas tau forms both static and diffusive patches along the microtubule lattice (Fig. S1K). The mean dwell time of MAP7 is 114.5 ± 6.16 s (n = 221 events from 11 recordings, two independent experiments), compared with 14.9 ± 1.19 s for tau (n = 128 events from 26 recordings, two independent experiments). C, force traces were acquired at 2 kHz and median-filtered at 20 Hz. We observe force events directed toward both the minus-end (i, iii, and vii) and plus-end (ii, v, and vi) and also bidirectional force events (iv and viii) (0 nm: n = 689 events from 38 recordings, 11 independent experiments; 10 nm MAP7: n = 787 events from 40 recordings, 11 independent experiments). D, maximum forces for all trap displacements greater than 300 ms (top) and 500 ms (bottom) in duration were included in the histogram. Consistent with previous results (14, 30), plus-end–directed force events consist of unitary stall forces of kinesin-1 and kinesin-2, events where the motors detach before reaching their stall force, and rare events driven by multiple kinesins. Minus-end–directed forces indicate events driven by teams of several dynein motors (Fig. S1C). The frequency and magnitude of kinesin-driven forces increase in the presence of 10 nm MAP7. In response, dynein-mediated forces are reduced. The Bayesian information criterion was used to determine the optimal number of components to describe the force histograms (Fig. S1F). Mean forces for plus-end directed motors are 1.57, 2.38, and 4.5 and for minus-ended motors are 1.14, 1.6, 2.8, and 5.8 pN. With MAP7, mean forces of the multicomponent fits for plus-end–directed forces are 1.4, 2.4, 4.5, and 7.3 pN, and for minus-end–directed forces, they are 1.4, 2.7, and ≥9 pN (p < 0.001; Kolmogorov–Smirnov test; Fig. S5A). E, teams of kinesin and dynein motors remain engaged to the microtubule under load for longer durations in the presence of MAP7. The color of the trajectory indicates the duration of a stall event. The duration of force events is significantly longer for kinesin-driven events with MAP7 (<T0 nM,+> = 1.5 s, <T10 nM,+> = 2.5 s, p < 0.01), whereas the duration of dynein-driven forces is slightly decreased (<T0 nM,−> = 2.26 s, <T10 nM,−> = 1.8 s, p = not significant) (Fig. S5C). F, comparing the duration of events of similar maximum force indicates that MAP7 does not alter the duration of events driven by similar numbers of motors. G, the relative binding rate was calculated as the reciprocal of the dwell time (green periods) preceding a force event (yellow). H, MAP7 increases the relative binding rate of plus-ended motors on MAP7 decorated microtubules by 28% (<π0 nM,+> = 0.89 s−1, <π10 nM,+> = 1.14 s−1; <π0 nM,−> = 1.05 s−1, <π10 nM,−> = 1.15 s−1). Error bars, S.E.
    Purification Map7, supplied by Addgene inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/purification map7/product/Addgene inc
    Average 90 stars, based on 1 article reviews
    purification map7 - by Bioz Stars, 2026-05
    90/100 stars
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    MAP7 targets bidirectional cargoes to the microtubule plus-end by increasing the number of engaged kinesin motors. A, isolated phagosomes containing fluorescent beads were positioned on polarity-marked microtubules, and the forces were measured using an optical trap. These isolated phagosomes are transported by teams of kinesin-1, kinesin-2, and dynein motors (14). B, MAP7 binds in static patches (Fig. S1J; Movie S6), whereas tau forms both static and diffusive patches along the microtubule lattice (Fig. S1K). The mean dwell time of MAP7 is 114.5 ± 6.16 s (n = 221 events from 11 recordings, two independent experiments), compared with 14.9 ± 1.19 s for tau (n = 128 events from 26 recordings, two independent experiments). C, force traces were acquired at 2 kHz and median-filtered at 20 Hz. We observe force events directed toward both the minus-end (i, iii, and vii) and plus-end (ii, v, and vi) and also bidirectional force events (iv and viii) (0 nm: n = 689 events from 38 recordings, 11 independent experiments; 10 nm MAP7: n = 787 events from 40 recordings, 11 independent experiments). D, maximum forces for all trap displacements greater than 300 ms (top) and 500 ms (bottom) in duration were included in the histogram. Consistent with previous results (14, 30), plus-end–directed force events consist of unitary stall forces of kinesin-1 and kinesin-2, events where the motors detach before reaching their stall force, and rare events driven by multiple kinesins. Minus-end–directed forces indicate events driven by teams of several dynein motors (Fig. S1C). The frequency and magnitude of kinesin-driven forces increase in the presence of 10 nm MAP7. In response, dynein-mediated forces are reduced. The Bayesian information criterion was used to determine the optimal number of components to describe the force histograms (Fig. S1F). Mean forces for plus-end directed motors are 1.57, 2.38, and 4.5 and for minus-ended motors are 1.14, 1.6, 2.8, and 5.8 pN. With MAP7, mean forces of the multicomponent fits for plus-end–directed forces are 1.4, 2.4, 4.5, and 7.3 pN, and for minus-end–directed forces, they are 1.4, 2.7, and ≥9 pN (p < 0.001; Kolmogorov–Smirnov test; Fig. S5A). E, teams of kinesin and dynein motors remain engaged to the microtubule under load for longer durations in the presence of MAP7. The color of the trajectory indicates the duration of a stall event. The duration of force events is significantly longer for kinesin-driven events with MAP7 (<T0 nM,+> = 1.5 s, <T10 nM,+> = 2.5 s, p < 0.01), whereas the duration of dynein-driven forces is slightly decreased (<T0 nM,−> = 2.26 s, <T10 nM,−> = 1.8 s, p = not significant) (Fig. S5C). F, comparing the duration of events of similar maximum force indicates that MAP7 does not alter the duration of events driven by similar numbers of motors. G, the relative binding rate was calculated as the reciprocal of the dwell time (green periods) preceding a force event (yellow). H, MAP7 increases the relative binding rate of plus-ended motors on MAP7 decorated microtubules by 28% (<π0 nM,+> = 0.89 s−1, <π10 nM,+> = 1.14 s−1; <π0 nM,−> = 1.05 s−1, <π10 nM,−> = 1.15 s−1). Error bars, S.E.

    Journal: The Journal of Biological Chemistry

    Article Title: MAP7 regulates organelle transport by recruiting kinesin-1 to microtubules

    doi: 10.1074/jbc.RA119.008052

    Figure Lengend Snippet: MAP7 targets bidirectional cargoes to the microtubule plus-end by increasing the number of engaged kinesin motors. A, isolated phagosomes containing fluorescent beads were positioned on polarity-marked microtubules, and the forces were measured using an optical trap. These isolated phagosomes are transported by teams of kinesin-1, kinesin-2, and dynein motors (14). B, MAP7 binds in static patches (Fig. S1J; Movie S6), whereas tau forms both static and diffusive patches along the microtubule lattice (Fig. S1K). The mean dwell time of MAP7 is 114.5 ± 6.16 s (n = 221 events from 11 recordings, two independent experiments), compared with 14.9 ± 1.19 s for tau (n = 128 events from 26 recordings, two independent experiments). C, force traces were acquired at 2 kHz and median-filtered at 20 Hz. We observe force events directed toward both the minus-end (i, iii, and vii) and plus-end (ii, v, and vi) and also bidirectional force events (iv and viii) (0 nm: n = 689 events from 38 recordings, 11 independent experiments; 10 nm MAP7: n = 787 events from 40 recordings, 11 independent experiments). D, maximum forces for all trap displacements greater than 300 ms (top) and 500 ms (bottom) in duration were included in the histogram. Consistent with previous results (14, 30), plus-end–directed force events consist of unitary stall forces of kinesin-1 and kinesin-2, events where the motors detach before reaching their stall force, and rare events driven by multiple kinesins. Minus-end–directed forces indicate events driven by teams of several dynein motors (Fig. S1C). The frequency and magnitude of kinesin-driven forces increase in the presence of 10 nm MAP7. In response, dynein-mediated forces are reduced. The Bayesian information criterion was used to determine the optimal number of components to describe the force histograms (Fig. S1F). Mean forces for plus-end directed motors are 1.57, 2.38, and 4.5 and for minus-ended motors are 1.14, 1.6, 2.8, and 5.8 pN. With MAP7, mean forces of the multicomponent fits for plus-end–directed forces are 1.4, 2.4, 4.5, and 7.3 pN, and for minus-end–directed forces, they are 1.4, 2.7, and ≥9 pN (p < 0.001; Kolmogorov–Smirnov test; Fig. S5A). E, teams of kinesin and dynein motors remain engaged to the microtubule under load for longer durations in the presence of MAP7. The color of the trajectory indicates the duration of a stall event. The duration of force events is significantly longer for kinesin-driven events with MAP7 ( = 1.5 s, = 2.5 s, p < 0.01), whereas the duration of dynein-driven forces is slightly decreased ( = 2.26 s, = 1.8 s, p = not significant) (Fig. S5C). F, comparing the duration of events of similar maximum force indicates that MAP7 does not alter the duration of events driven by similar numbers of motors. G, the relative binding rate was calculated as the reciprocal of the dwell time (green periods) preceding a force event (yellow). H, MAP7 increases the relative binding rate of plus-ended motors on MAP7 decorated microtubules by 28% (<π0 nM,+> = 0.89 s−1, <π10 nM,+> = 1.14 s−1; <π0 nM,−> = 1.05 s−1, <π10 nM,−> = 1.15 s−1). Error bars, S.E.

    Article Snippet: MAP7 expression and purification MAP7 (accession number {"type":"entrez-nucleotide","attrs":{"text":"BC052637","term_id":"30962906","term_text":"BC052637"}} BC052637 ) was cloned from pEGFP-MAP7 (Addgene plasmid 46076) into the baculovirus expression vector pFastBac with N-terminal FLAG and SNAP tags.

    Techniques: Isolation, Binding Assay

    MAP7 recruits kinesin-1 to microtubules. A and B, MAP7 recruits full-length kinesin-1 to microtubules in a dose-dependent manner (see also Fig. S2B). MgADP-bound kinesin-1 is in a weakly bound state. Kinesin-1 hydrolyzes MgATP to drive processive movement. C, when present at high levels, MAP7 increases kinesin-1 run lengths by up to ∼30%, possibly due to rapid re-attachment (average run length: 0 nm = 2033 ± 493.8 nm; 5 nm = 1640 ± 463 nm; 10 nm = 1800 ± 937 nm; 25 nm = 2227 ± 411.2 nm; 75 nm = 3002 ± 265.5 nm). D, the frequency of both processive and diffusive motility of kinesin-1 increases to a similar degree with increasing MAP7 concentration (0 nm MAP7: n = 15 events, three recordings; 5 nm MAP7: n = 17 events from three recordings; 10 nm MAP7: n = 21 events from three recordings; 25 nm MAP7: n = 37 events from three recordings; 75 nm MAP7: n = 70 events from three recordings). E and F, beads transported by ∼1–2 kinesin-1 motors were positioned on the microtubule using a weak optical trap (k ∼0.004 pN/nm) and imaged as they moved along the microtubule. G, long, directed events toward the microtubule plus-end indicate motility by multiple kinesin-1 motors. H, teams of kinesin-1 motors are more processive on MAP7-decorated microtubule (I and J). The average run length of kinesin-1 motors with MAP7 increases by ∼8-fold (average run length (0 nm) = 595 ± 60 nm; average run length (10 nm) = 5320 ± 890 nm), whereas the velocity is unaffected (average velocity (0 nm) = 220 ± 16 nm/s; average velocity (10 nm) = 292 ± 45 nm/s) (0 nm: n = 72 events from 21 trajectories, two independent experiments; 10 nm MAP7: n = 32 events from 18 trajectories, two independent experiments). Error bars, S.E.

    Journal: The Journal of Biological Chemistry

    Article Title: MAP7 regulates organelle transport by recruiting kinesin-1 to microtubules

    doi: 10.1074/jbc.RA119.008052

    Figure Lengend Snippet: MAP7 recruits kinesin-1 to microtubules. A and B, MAP7 recruits full-length kinesin-1 to microtubules in a dose-dependent manner (see also Fig. S2B). MgADP-bound kinesin-1 is in a weakly bound state. Kinesin-1 hydrolyzes MgATP to drive processive movement. C, when present at high levels, MAP7 increases kinesin-1 run lengths by up to ∼30%, possibly due to rapid re-attachment (average run length: 0 nm = 2033 ± 493.8 nm; 5 nm = 1640 ± 463 nm; 10 nm = 1800 ± 937 nm; 25 nm = 2227 ± 411.2 nm; 75 nm = 3002 ± 265.5 nm). D, the frequency of both processive and diffusive motility of kinesin-1 increases to a similar degree with increasing MAP7 concentration (0 nm MAP7: n = 15 events, three recordings; 5 nm MAP7: n = 17 events from three recordings; 10 nm MAP7: n = 21 events from three recordings; 25 nm MAP7: n = 37 events from three recordings; 75 nm MAP7: n = 70 events from three recordings). E and F, beads transported by ∼1–2 kinesin-1 motors were positioned on the microtubule using a weak optical trap (k ∼0.004 pN/nm) and imaged as they moved along the microtubule. G, long, directed events toward the microtubule plus-end indicate motility by multiple kinesin-1 motors. H, teams of kinesin-1 motors are more processive on MAP7-decorated microtubule (I and J). The average run length of kinesin-1 motors with MAP7 increases by ∼8-fold (average run length (0 nm) = 595 ± 60 nm; average run length (10 nm) = 5320 ± 890 nm), whereas the velocity is unaffected (average velocity (0 nm) = 220 ± 16 nm/s; average velocity (10 nm) = 292 ± 45 nm/s) (0 nm: n = 72 events from 21 trajectories, two independent experiments; 10 nm MAP7: n = 32 events from 18 trajectories, two independent experiments). Error bars, S.E.

    Article Snippet: MAP7 expression and purification MAP7 (accession number {"type":"entrez-nucleotide","attrs":{"text":"BC052637","term_id":"30962906","term_text":"BC052637"}} BC052637 ) was cloned from pEGFP-MAP7 (Addgene plasmid 46076) into the baculovirus expression vector pFastBac with N-terminal FLAG and SNAP tags.

    Techniques: Concentration Assay

    MAP7 increases the forces generated by teams of kinesin-1. We measured forces by single kinesin-1 motors and teams at three motor densities (ratio of motors to beads in the conjugation reaction). A, 3300 kinesin-1s/bead resulted in motility driven by a single kinesin-1, where <50% of beads interacted with the microtubule; G, 6600 kinesin-1s/bead resulted in motility due to 1–2 engaged kinesin-1 motors; M, 13,000 kinesin-1s/bead resulted in 2–3 kinesin-1 motors. B and C, on beads driven by single kinesin-1 motors, force distributions indicate unitary stall force of kinesin-1 and substall detachment forces (mean forces of the multicomponent fits Fcomp = 1.3 and 4.03 pN). With the addition of MAP7, substall detachment events decrease, and the frequency of unitary stall force events due to single kinesin-1 increases (Fcomp = 4.23 and ≥9 pN) (p < 0.001; Kolmogorov–Smirnov test; Fig. S5B) (0 nm: n = 444 events from 25 recordings, four independent experiments; 10 nm MAP7: n = 536 events from 25 recordings, four independent experiments). H and I, on beads driven by ∼1–2 kinesin-1s, force distributions show three distinct populations: forces at unitary stall force of kinesin-1, detachment forces, and rare multimotor events (Fcomp = 1.27, 3.47, and 7 pN). With the addition of MAP7, detachment and low force events decrease, whereas the frequency of unitary stall force events increases (Fcomp = 1.17, 4, and 7 pN) (p < 0.001; Kolmogorov–Smirnov test; Fig. S5B). The frequency and magnitude of multimotor force events remain unchanged (0 nm: n = 479 events from 26 recordings, four independent experiments; 10 nm MAP7: n = 623 events from 24 recordings, four independent experiments). N and O, on beads driven by ∼2–3 kinesin-1 motors, force distribution shows three distinct populations: forces at unitary stall force of kinesin-1, low-force events, and multimotor events (Fcomp = 1.24, 3.64, and 7.5 pN). With MAP7, we observe a shift toward frequent high-force events driven by multiple engaged kinesin-1s (Fcomp = 4.24, 5.97, and 7.29) (p < 0.001; Kolmogorov–Smirnov test; Fig. S5B) (0 nm: n = 485 events from 23 recordings, three independent experiments; 10 nm MAP7: n = 378 events from 22 recordings, three independent experiments). D, J, P, and Fig. S3, the duration of stall events at a given force is not strongly influenced by MAP7, indicating that MAP7 does not affect the processivity of single kinesin motors. Single kinesin-1 motors (E) and teams of 1–2 kinesin-1 motors (K) bind much faster to MAP7-decorated microtubules. Q, the increase in binding rate is not observed for larger teams of 2–3 kinesin-1s, likely because attachment is no longer limited by the single-motor binding rate when many motors are available for binding (single kinesin-1: 0 nm = 0.77 s−1 and 10 nm = 0.95 s−1; teams of ∼1–2 kinesin-1s: 0 nm = 1.04 s−1 and 10 nm = 1.55 s−1; ∼2–3 kinesin-1s: 0 nm = 1.24 s−1 and 10 nm = 1.35 s−1). F, L, R, the force–velocity curves indicate that more kinesin-1 motors are simultaneously engaged when MAP7 is present, as indicated by higher velocities at the same load. Error bars, S.E.

    Journal: The Journal of Biological Chemistry

    Article Title: MAP7 regulates organelle transport by recruiting kinesin-1 to microtubules

    doi: 10.1074/jbc.RA119.008052

    Figure Lengend Snippet: MAP7 increases the forces generated by teams of kinesin-1. We measured forces by single kinesin-1 motors and teams at three motor densities (ratio of motors to beads in the conjugation reaction). A, 3300 kinesin-1s/bead resulted in motility driven by a single kinesin-1, where <50% of beads interacted with the microtubule; G, 6600 kinesin-1s/bead resulted in motility due to 1–2 engaged kinesin-1 motors; M, 13,000 kinesin-1s/bead resulted in 2–3 kinesin-1 motors. B and C, on beads driven by single kinesin-1 motors, force distributions indicate unitary stall force of kinesin-1 and substall detachment forces (mean forces of the multicomponent fits Fcomp = 1.3 and 4.03 pN). With the addition of MAP7, substall detachment events decrease, and the frequency of unitary stall force events due to single kinesin-1 increases (Fcomp = 4.23 and ≥9 pN) (p < 0.001; Kolmogorov–Smirnov test; Fig. S5B) (0 nm: n = 444 events from 25 recordings, four independent experiments; 10 nm MAP7: n = 536 events from 25 recordings, four independent experiments). H and I, on beads driven by ∼1–2 kinesin-1s, force distributions show three distinct populations: forces at unitary stall force of kinesin-1, detachment forces, and rare multimotor events (Fcomp = 1.27, 3.47, and 7 pN). With the addition of MAP7, detachment and low force events decrease, whereas the frequency of unitary stall force events increases (Fcomp = 1.17, 4, and 7 pN) (p < 0.001; Kolmogorov–Smirnov test; Fig. S5B). The frequency and magnitude of multimotor force events remain unchanged (0 nm: n = 479 events from 26 recordings, four independent experiments; 10 nm MAP7: n = 623 events from 24 recordings, four independent experiments). N and O, on beads driven by ∼2–3 kinesin-1 motors, force distribution shows three distinct populations: forces at unitary stall force of kinesin-1, low-force events, and multimotor events (Fcomp = 1.24, 3.64, and 7.5 pN). With MAP7, we observe a shift toward frequent high-force events driven by multiple engaged kinesin-1s (Fcomp = 4.24, 5.97, and 7.29) (p < 0.001; Kolmogorov–Smirnov test; Fig. S5B) (0 nm: n = 485 events from 23 recordings, three independent experiments; 10 nm MAP7: n = 378 events from 22 recordings, three independent experiments). D, J, P, and Fig. S3, the duration of stall events at a given force is not strongly influenced by MAP7, indicating that MAP7 does not affect the processivity of single kinesin motors. Single kinesin-1 motors (E) and teams of 1–2 kinesin-1 motors (K) bind much faster to MAP7-decorated microtubules. Q, the increase in binding rate is not observed for larger teams of 2–3 kinesin-1s, likely because attachment is no longer limited by the single-motor binding rate when many motors are available for binding (single kinesin-1: 0 nm = 0.77 s−1 and 10 nm = 0.95 s−1; teams of ∼1–2 kinesin-1s: 0 nm = 1.04 s−1 and 10 nm = 1.55 s−1; ∼2–3 kinesin-1s: 0 nm = 1.24 s−1 and 10 nm = 1.35 s−1). F, L, R, the force–velocity curves indicate that more kinesin-1 motors are simultaneously engaged when MAP7 is present, as indicated by higher velocities at the same load. Error bars, S.E.

    Article Snippet: MAP7 expression and purification MAP7 (accession number {"type":"entrez-nucleotide","attrs":{"text":"BC052637","term_id":"30962906","term_text":"BC052637"}} BC052637 ) was cloned from pEGFP-MAP7 (Addgene plasmid 46076) into the baculovirus expression vector pFastBac with N-terminal FLAG and SNAP tags.

    Techniques: Generated, Conjugation Assay, Binding Assay

    MAP7 directs transport toward the microtubule plus-end. A, we extended the mathematical model proposed by Muller et al. (40) to describe the interaction between teams of kinesin-1, kinesin-2, and dynein motors based on single-motor parameters including the motor stall force, detachment force, and unbinding and binding rates (14). We modeled the effect of MAP7 by increasing the binding rate of single kinesin-1 molecules by the same amount as we measured in optical trapping measurements. Kinesin-2 and dynein were assumed to be unaffected by MAP7. B, the increase in kinesin-1 binding rate biases simulated trajectories toward the plus-end (number of simulated trajectories, n = 100). C, we calculated run length as distance between reversals (29) and consider events >400 nm as processive. Plus-end–directed run lengths increase by ∼24%, whereas minus-end–directed run lengths decrease by ∼24%. D, the model results suggest that the shift in phagosome transport toward the microtubule plus-end that we observe can be described by simply increasing the kinesin-1 binding rate with no direct effect on kinesin-2 or dynein. E, the number of engaged kinesin and dynein motors changes in the presence of MAP7. A greater number of plus-ended motors are simultaneously engaged and exerting force, and as a result, minus-ended motors are under higher loads and are less processive. F, MAP7 and tau exhibit distinct localizations in neurons. Whereas MAP7 is enriched at axonal branches (21), tau is localized in a gradient along the axon. Thus, MAP7 might target cargoes to the microtubule plus-end at branch sites, whereas tau directs distal cargoes toward the cell body. Error bars, S.E.

    Journal: The Journal of Biological Chemistry

    Article Title: MAP7 regulates organelle transport by recruiting kinesin-1 to microtubules

    doi: 10.1074/jbc.RA119.008052

    Figure Lengend Snippet: MAP7 directs transport toward the microtubule plus-end. A, we extended the mathematical model proposed by Muller et al. (40) to describe the interaction between teams of kinesin-1, kinesin-2, and dynein motors based on single-motor parameters including the motor stall force, detachment force, and unbinding and binding rates (14). We modeled the effect of MAP7 by increasing the binding rate of single kinesin-1 molecules by the same amount as we measured in optical trapping measurements. Kinesin-2 and dynein were assumed to be unaffected by MAP7. B, the increase in kinesin-1 binding rate biases simulated trajectories toward the plus-end (number of simulated trajectories, n = 100). C, we calculated run length as distance between reversals (29) and consider events >400 nm as processive. Plus-end–directed run lengths increase by ∼24%, whereas minus-end–directed run lengths decrease by ∼24%. D, the model results suggest that the shift in phagosome transport toward the microtubule plus-end that we observe can be described by simply increasing the kinesin-1 binding rate with no direct effect on kinesin-2 or dynein. E, the number of engaged kinesin and dynein motors changes in the presence of MAP7. A greater number of plus-ended motors are simultaneously engaged and exerting force, and as a result, minus-ended motors are under higher loads and are less processive. F, MAP7 and tau exhibit distinct localizations in neurons. Whereas MAP7 is enriched at axonal branches (21), tau is localized in a gradient along the axon. Thus, MAP7 might target cargoes to the microtubule plus-end at branch sites, whereas tau directs distal cargoes toward the cell body. Error bars, S.E.

    Article Snippet: MAP7 expression and purification MAP7 (accession number {"type":"entrez-nucleotide","attrs":{"text":"BC052637","term_id":"30962906","term_text":"BC052637"}} BC052637 ) was cloned from pEGFP-MAP7 (Addgene plasmid 46076) into the baculovirus expression vector pFastBac with N-terminal FLAG and SNAP tags.

    Techniques: Binding Assay