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Asymmetric tails of actin filament networks generated by incubating Ni-functionalized and fluorescent lipid-coated beads with His-VVCA (N-WASP), followed by addition of 100 <t>nM</t> <t>Arp2/3</t> complex, 5 µM profilin-actin, and 50 nM CP for 30 min (top row). Addition of 500 nM V-1 to the reaction mixture resulted in F-actin growing from the bead surface as a symmetric ring and a diffuse cloud around the bead (second row). Addition of low concentrations of His-CBR126 resulted in asymmetric F-actin tail growth from the bead (rows labeled 35 nM and 50 nM), and higher concentrations inhibited actin growth (row labeled 2000 nM).
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Asymmetric tails of actin filament networks generated by incubating Ni-functionalized and fluorescent lipid-coated beads with His-VVCA (N-WASP), followed by addition of 100 nM Arp2/3 complex, 5 µM profilin-actin, and 50 nM CP for 30 min (top row). Addition of 500 nM V-1 to the reaction mixture resulted in F-actin growing from the bead surface as a symmetric ring and a diffuse cloud around the bead (second row). Addition of low concentrations of His-CBR126 resulted in asymmetric F-actin tail growth from the bead (rows labeled 35 nM and 50 nM), and higher concentrations inhibited actin growth (row labeled 2000 nM).

Journal: bioRxiv

Article Title: Biochemical Functions of the Membrane-Binding Domain of CARMIL

doi: 10.64898/2026.01.05.697744

Figure Lengend Snippet: Asymmetric tails of actin filament networks generated by incubating Ni-functionalized and fluorescent lipid-coated beads with His-VVCA (N-WASP), followed by addition of 100 nM Arp2/3 complex, 5 µM profilin-actin, and 50 nM CP for 30 min (top row). Addition of 500 nM V-1 to the reaction mixture resulted in F-actin growing from the bead surface as a symmetric ring and a diffuse cloud around the bead (second row). Addition of low concentrations of His-CBR126 resulted in asymmetric F-actin tail growth from the bead (rows labeled 35 nM and 50 nM), and higher concentrations inhibited actin growth (row labeled 2000 nM).

Article Snippet: Porcine brain Arp2/3 complex from Cytoskeleton (Cat. No. RP01P, Denver, CO) was reconstituted per manufacturer instructions and used within one month.

Techniques: Generated, Labeling

A. His-tagged MB mutants cause actin network to grow asymmetrically from the bead surface in a mixture of 100 nM Arp2/3 complex, 5 µM profilin-actin, 50 nM CP, and 500 nM V-1 (30-minute time points) similar to His-CBR126 wt. B. Untethered CBR126 associates with the lipid beads via the MB domain and displays more robust asymmetric actin growth than tethered His-CBR126. MB mutants do not associate with the lipid beads and do not show the same effects on the actin network.

Journal: bioRxiv

Article Title: Biochemical Functions of the Membrane-Binding Domain of CARMIL

doi: 10.64898/2026.01.05.697744

Figure Lengend Snippet: A. His-tagged MB mutants cause actin network to grow asymmetrically from the bead surface in a mixture of 100 nM Arp2/3 complex, 5 µM profilin-actin, 50 nM CP, and 500 nM V-1 (30-minute time points) similar to His-CBR126 wt. B. Untethered CBR126 associates with the lipid beads via the MB domain and displays more robust asymmetric actin growth than tethered His-CBR126. MB mutants do not associate with the lipid beads and do not show the same effects on the actin network.

Article Snippet: Porcine brain Arp2/3 complex from Cytoskeleton (Cat. No. RP01P, Denver, CO) was reconstituted per manufacturer instructions and used within one month.

Techniques:

CP bound to V-1 in the cytoplasm is inactive. 2. CP / V-1 binding to CARMIL promotes V-1 dissociation. 3. Free CP binds barbed ends and promotes Arp2/3-nucleated polarized actin growth at the bead surface. 4 & 5. Near the bead surface, CARMIL can a) promote uncapping of a capped barbed end to allow filament growth or b) capture a capped actin filament. Dynamic association of CP with barbed end - “loose / leaky” capper. 6. Dynamic association of CARMIL with lipid: CARMIL can leave the bead surface and stay bound to CP as the actin filament network grows and flows away from the bead surface.

Journal: bioRxiv

Article Title: Biochemical Functions of the Membrane-Binding Domain of CARMIL

doi: 10.64898/2026.01.05.697744

Figure Lengend Snippet: CP bound to V-1 in the cytoplasm is inactive. 2. CP / V-1 binding to CARMIL promotes V-1 dissociation. 3. Free CP binds barbed ends and promotes Arp2/3-nucleated polarized actin growth at the bead surface. 4 & 5. Near the bead surface, CARMIL can a) promote uncapping of a capped barbed end to allow filament growth or b) capture a capped actin filament. Dynamic association of CP with barbed end - “loose / leaky” capper. 6. Dynamic association of CARMIL with lipid: CARMIL can leave the bead surface and stay bound to CP as the actin filament network grows and flows away from the bead surface.

Article Snippet: Porcine brain Arp2/3 complex from Cytoskeleton (Cat. No. RP01P, Denver, CO) was reconstituted per manufacturer instructions and used within one month.

Techniques: Binding Assay