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cul4a ![Lgl physically interacts with VprBP and DDB1 independently of <t>Cul4A.</t> (A) Lgl2 was immunoprecipitated from lysate prepared from confluently cultured MDCK cells. VprBP and DDB1 were coprecipitated with Lgl2, along with aPKC and PAR6β. (B) VprBP was immunoprecipitated from lysate prepared from confluently cultured MDCK cells. Lgl2, Lgl1, DDB1, and <t>Cul4A</t> were coprecipitated with VprBP, whereas aPKC and PAR6β were not. (C) VprBP was immunoprecipitated from control and Lgl1/2 KD MDCK cell lysate. Coimmunoprecipitation of Cul4A was up-regulated by depletion of Lgl1/2. (D) V5-VprBP deletion mutants and HA-Lgl2 were coexpressed in HEK293T cells. Immunoprecipitation was performed using anti-V5 antibody conjugated resin. Asterisk indicates the 110-kDa bands that were reproducibly detected in this experiment. VprBP may have an endo-cleavage site around amino acid 964. (E) Schematic representation of VprBP mutants and results of the experiment performed in D. Numbers in the left column represent amino acid number. Asterisk indicates position of amino acid 964. The binding site of Merlin, reported in Li et al. (2010) , is also illustrated. (F) VprBP was immunoprecipitated from the lysates of HEK293T cells transfected with SBP-Lgl2 expression vector (lanes 2 and 4) or SBP expression vector (lanes 1 and 3). Note that the amount of Cul4A coimmunoprecipitated with VprBP was significantly decreased by expression of Lgl2. (G) Coimmunoprecipitated DDB1 and Cul4A were quantified by densitometry, and the average of three independent experiments is plotted. Error bars indicate ±SD. Double asterisks denotes significant difference ( p < 0.01) by Student's t test. (H) VprBP or Cdt2 was immunoprecipitated from the common lysate of HEK293T cells transfected with SBP-Lgl2 expression vector (lanes 2, 4, 6, and 8) and also immunoprecipitated from the common lysate of cells transfected with SBP expression vector (lanes 1, 3, 5, and 7). Long-exposure image is also presented for Cul4A-immunoblot. (I) Hypothetical model for CRL4 [VprBP] and Lgl-VprBP-DDB1 complex. Lgl2 may sterically mask the Cul4A-binding domain of DDB1.](https://pub-med-central-images-cdn.bioz.com/pub_med_central_ids_ending_with_1298/pmc04571298/pmc04571298__2426fig3.jpg) Cul4a, supplied by Proteintech, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more https://www.bioz.com/result/cul4a/product/Proteintech Average 93 stars, based on 1 article reviews
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Image Search Results
Journal: Molecular cell
Article Title: PIKES Analysis Reveals Response to Degraders and Key Regulatory Mechanisms of the CRL4 Network.
doi: 10.1016/j.molcel.2019.12.013
Figure Lengend Snippet: Figure 1. A Toolbox to Monitor Endogenous CRL4 Complexes Schematic representation of the PIKES approach: (1) 293T/17 cells were genetically engineered to carry a 3xFLAG or 3xHA on Cul4A or Cul4B or both to enable rapid and efficient (2) immunoprecipitation of endogenous CRL4 assemblages. (3) Endogenous CRL4 ligase complexes were then evaluated systematically using global and targeted proteomic approaches. First, the protein interaction network of interest was analyzed at endogenous protein levels, followed by a kinetic characterization of interactions, and the development of chemical and biochemical methods to control and preserve the composition of protein complexes. Subsequently, the cellular concentrations and complex stoichiometries were analyzed using QconCAT standards, and induced changes in complex composition were monitored quantitatively. See also Figures S1, S7, and S8.
Article Snippet: REAGENT or
Techniques: Immunoprecipitation, Control
Journal: Molecular cell
Article Title: PIKES Analysis Reveals Response to Degraders and Key Regulatory Mechanisms of the CRL4 Network.
doi: 10.1016/j.molcel.2019.12.013
Figure Lengend Snippet: Figure 3. Individual CRL4 Ligases Show Cullin-Scaffold Preferences and Differ up to 100-Fold in Absolute Abundance (A) Schematic of CRL4 QconCAT experiments to determine cellular concentrations and complex stoichiometries. (B–D) Absolute quantification of CRL4 components in whole cell lysates as well as immunoprecipitated Cul4 complexes. *Cul4 scaffolds were measured by targeting peptides common (cP) or unique (uP) to Cul4A and Cul4B. (E) Summary of cellular organization of CRL4 complexes. (F) and (G) Cellular concentrations of assembled CRL4s as well as DCAFs. (H) Correlation plot of percentage assembled (percentage of DCAF Cul4-bound versus free) and CRL4 ligase abundance (percentage of individual Cul4DCAF
Article Snippet: REAGENT or
Techniques: Immunoprecipitation
Journal: Molecular Biology of the Cell
Article Title: Tumor suppressor protein Lgl mediates G1 cell cycle arrest at high cell density by forming an Lgl-VprBP-DDB1 complex
doi: 10.1091/mbc.E14-10-1462
Figure Lengend Snippet: Lgl physically interacts with VprBP and DDB1 independently of Cul4A. (A) Lgl2 was immunoprecipitated from lysate prepared from confluently cultured MDCK cells. VprBP and DDB1 were coprecipitated with Lgl2, along with aPKC and PAR6β. (B) VprBP was immunoprecipitated from lysate prepared from confluently cultured MDCK cells. Lgl2, Lgl1, DDB1, and Cul4A were coprecipitated with VprBP, whereas aPKC and PAR6β were not. (C) VprBP was immunoprecipitated from control and Lgl1/2 KD MDCK cell lysate. Coimmunoprecipitation of Cul4A was up-regulated by depletion of Lgl1/2. (D) V5-VprBP deletion mutants and HA-Lgl2 were coexpressed in HEK293T cells. Immunoprecipitation was performed using anti-V5 antibody conjugated resin. Asterisk indicates the 110-kDa bands that were reproducibly detected in this experiment. VprBP may have an endo-cleavage site around amino acid 964. (E) Schematic representation of VprBP mutants and results of the experiment performed in D. Numbers in the left column represent amino acid number. Asterisk indicates position of amino acid 964. The binding site of Merlin, reported in Li et al. (2010) , is also illustrated. (F) VprBP was immunoprecipitated from the lysates of HEK293T cells transfected with SBP-Lgl2 expression vector (lanes 2 and 4) or SBP expression vector (lanes 1 and 3). Note that the amount of Cul4A coimmunoprecipitated with VprBP was significantly decreased by expression of Lgl2. (G) Coimmunoprecipitated DDB1 and Cul4A were quantified by densitometry, and the average of three independent experiments is plotted. Error bars indicate ±SD. Double asterisks denotes significant difference ( p < 0.01) by Student's t test. (H) VprBP or Cdt2 was immunoprecipitated from the common lysate of HEK293T cells transfected with SBP-Lgl2 expression vector (lanes 2, 4, 6, and 8) and also immunoprecipitated from the common lysate of cells transfected with SBP expression vector (lanes 1, 3, 5, and 7). Long-exposure image is also presented for Cul4A-immunoblot. (I) Hypothetical model for CRL4 [VprBP] and Lgl-VprBP-DDB1 complex. Lgl2 may sterically mask the Cul4A-binding domain of DDB1.
Article Snippet: Other antibodies were purchased as follows: Lgl2 (Abnova, Taipei, Taiwan), Lgl1 (Sigma-Aldrich, St. Louis, MO), VprBP (Proteintech Group, Chicago, IL), DDB1 (Bethyl, Montgomery, TX),
Techniques: Immunoprecipitation, Cell Culture, Control, Binding Assay, Transfection, Expressing, Plasmid Preparation, Western Blot
Journal: Molecular Biology of the Cell
Article Title: Tumor suppressor protein Lgl mediates G1 cell cycle arrest at high cell density by forming an Lgl-VprBP-DDB1 complex
doi: 10.1091/mbc.E14-10-1462
Figure Lengend Snippet: VprBP is involved in suppression of overproliferation mediated by Lgl. (A) MDCK cells were transfected with the indicated siRNAs, stained with PI, and subjected to flow cytometry. (B) MDCK cells were transfected with siRNAs for VprBP or DDB1 and cultured at low density. Knockdown of VprBP or DDB1 up-regulated p27 and down-regulated Skp2. (C) MDCK cells were transfected with two siRNAs targeting for Cul4A and Cul4B and cultured at low density. Asterisk denotes nonspecific signal. (D) VprBP and Cdh1 were simultaneously knocked down in MDCK cells. Note that knockdown of Cdh1 alleviated the effects of VprBP knockdown. (E) Control or Lgl1/2 KD MDCK cells were transfected with siRNA for VprBP. After culturing for 2 d, the amounts of Skp2 and p27 were analyzed. (F) Control or Lgl1/2 KD MDCK cells were transfected with nonsilencing siRNA (NS) or siRNA for VprBP and seeded confluently to Transwells. After culturing for 2 d, the BrdU incorporation assay was performed. (G) The ratio of BrdU-positive cells to total cells in the experiment in F was determined, and averages of three independent experiments are plotted. Error bars indicate ±SD. Asterisk denotes significant difference ( p < 0.05) by Student's t test. (H) Control or Lgl1/2 KD MDCK cells were transfected with nonsilencing siRNA (NS) or siRNA for VprBP and cultured until they reached confluency. Phase-contrast images and reconstituted confocal z -axis images of the epithelial sheets. Samples were stained with anti–ZO-1 (green), Alexa 647–phalloidin (red), and PI (blue). Scale bars, 10 μm (white), 30 μm (black). (I) The ratio of area of foci to total area was determined, and averages of three independent experiments are plotted. Error bars indicate ±SD. Note that knockdown of VprBP significantly suppressed formation of multilayered structures in Lgl1/2 KD MDCK cells. (J) Control or Lgl1/2 KD MDCK cells were transfected with nonsilencing siRNA (NS) or Cul4A siRNA 1 and Cul4B siRNA 1 and cultured until they reached confluency. Then the ratio of area of foci to total area was determined.
Article Snippet: Other antibodies were purchased as follows: Lgl2 (Abnova, Taipei, Taiwan), Lgl1 (Sigma-Aldrich, St. Louis, MO), VprBP (Proteintech Group, Chicago, IL), DDB1 (Bethyl, Montgomery, TX),
Techniques: Transfection, Staining, Flow Cytometry, Cell Culture, Knockdown, Control, BrdU Incorporation Assay
![Lgl2-VprBP-DDB1 complex was well formed with reduction of CRL4 [VprBP] complex in confluent cells. (A) Lgl2 was immunoprecipitated from the lysates of MDCK cells cultured in confluent or low-density conditions. The amount of coprecipitated VprBP was higher from confluent cells. (B) VprBP was immunoprecipitated from MDCK cell lysates cultured in confluent or low-density conditions. The amount of coprecipitated Cul4A was lower from confluent cells. (C) Hypothetical model of Lgl-mediated inhibition of the CRL4 [VprBP] complex and its downstream pathway. Lgl forms a complex with VprBP-DDB1 independently of Cul4A when cells reach confluency. Lgl-VprBP-DDB1 complex is catalytically inactive because it lacks Cul4A and Roc1, the active center that associates with E2 enzyme.](https://pub-med-central-images-cdn.bioz.com/pub_med_central_ids_ending_with_1298/pmc04571298/pmc04571298__2426fig5.jpg)
Journal: Molecular Biology of the Cell
Article Title: Tumor suppressor protein Lgl mediates G1 cell cycle arrest at high cell density by forming an Lgl-VprBP-DDB1 complex
doi: 10.1091/mbc.E14-10-1462
Figure Lengend Snippet: Lgl2-VprBP-DDB1 complex was well formed with reduction of CRL4 [VprBP] complex in confluent cells. (A) Lgl2 was immunoprecipitated from the lysates of MDCK cells cultured in confluent or low-density conditions. The amount of coprecipitated VprBP was higher from confluent cells. (B) VprBP was immunoprecipitated from MDCK cell lysates cultured in confluent or low-density conditions. The amount of coprecipitated Cul4A was lower from confluent cells. (C) Hypothetical model of Lgl-mediated inhibition of the CRL4 [VprBP] complex and its downstream pathway. Lgl forms a complex with VprBP-DDB1 independently of Cul4A when cells reach confluency. Lgl-VprBP-DDB1 complex is catalytically inactive because it lacks Cul4A and Roc1, the active center that associates with E2 enzyme.
Article Snippet: Other antibodies were purchased as follows: Lgl2 (Abnova, Taipei, Taiwan), Lgl1 (Sigma-Aldrich, St. Louis, MO), VprBP (Proteintech Group, Chicago, IL), DDB1 (Bethyl, Montgomery, TX),
Techniques: Immunoprecipitation, Cell Culture, Inhibition
Journal: Molecular cell
Article Title: PIKES Analysis Reveals Response to Degraders and Key Regulatory Mechanisms of the CRL4 Network.
doi: 10.1016/j.molcel.2019.12.013
Figure Lengend Snippet: Figure 1. A Toolbox to Monitor Endogenous CRL4 Complexes Schematic representation of the PIKES approach: (1) 293T/17 cells were genetically engineered to carry a 3xFLAG or 3xHA on Cul4A or Cul4B or both to enable rapid and efficient (2) immunoprecipitation of endogenous CRL4 assemblages. (3) Endogenous CRL4 ligase complexes were then evaluated systematically using global and targeted proteomic approaches. First, the protein interaction network of interest was analyzed at endogenous protein levels, followed by a kinetic characterization of interactions, and the development of chemical and biochemical methods to control and preserve the composition of protein complexes. Subsequently, the cellular concentrations and complex stoichiometries were analyzed using QconCAT standards, and induced changes in complex composition were monitored quantitatively. See also Figures S1, S7, and S8.
Article Snippet: REAGENT or
Techniques: Immunoprecipitation, Control
Journal: Molecular cell
Article Title: PIKES Analysis Reveals Response to Degraders and Key Regulatory Mechanisms of the CRL4 Network.
doi: 10.1016/j.molcel.2019.12.013
Figure Lengend Snippet: Figure 3. Individual CRL4 Ligases Show Cullin-Scaffold Preferences and Differ up to 100-Fold in Absolute Abundance (A) Schematic of CRL4 QconCAT experiments to determine cellular concentrations and complex stoichiometries. (B–D) Absolute quantification of CRL4 components in whole cell lysates as well as immunoprecipitated Cul4 complexes. *Cul4 scaffolds were measured by targeting peptides common (cP) or unique (uP) to Cul4A and Cul4B. (E) Summary of cellular organization of CRL4 complexes. (F) and (G) Cellular concentrations of assembled CRL4s as well as DCAFs. (H) Correlation plot of percentage assembled (percentage of DCAF Cul4-bound versus free) and CRL4 ligase abundance (percentage of individual Cul4DCAF
Article Snippet: REAGENT or
Techniques: Immunoprecipitation