4N78
The WAVE Regulatory Complex Links Diverse Receptors to the Actin Cytoskeleton
Summary for 4N78
| Entry DOI | 10.2210/pdb4n78/pdb |
| Related | 3P8C |
| Descriptor | Cytoplasmic FMR1-interacting protein 1, Nck-associated protein 1, Wiskott-Aldrich syndrome protein family member 1, ... (9 entities in total) |
| Functional Keywords | actin dynamics, protein binding |
| Biological source | Homo sapiens (human) More |
| Cellular location | Cytoplasm, perinuclear region (By similarity): Q7L576 Cell membrane; Single-pass membrane protein; Cytoplasmic side (By similarity): Q9Y2A7 Cytoplasm, cytoskeleton: Q92558 Cytoplasm, cytoskeleton (By similarity): J3KNB2 |
| Total number of polymer chains | 6 |
| Total formula weight | 403900.56 |
| Authors | Chen, Z.C. (deposition date: 2013-10-15, release date: 2014-02-05, Last modification date: 2024-02-28) |
| Primary citation | Chen, B.,Brinkmann, K.,Chen, Z.,Pak, C.W.,Liao, Y.,Shi, S.,Henry, L.,Grishin, N.V.,Bogdan, S.,Rosen, M.K. The WAVE Regulatory Complex Links Diverse Receptors to the Actin Cytoskeleton. Cell(Cambridge,Mass.), 156:195-207, 2014 Cited by PubMed Abstract: The WAVE regulatory complex (WRC) controls actin cytoskeletal dynamics throughout the cell by stimulating the actin-nucleating activity of the Arp2/3 complex at distinct membrane sites. However, the factors that recruit the WRC to specific locations remain poorly understood. Here, we have identified a large family of potential WRC ligands, consisting of ∼120 diverse membrane proteins, including protocadherins, ROBOs, netrin receptors, neuroligins, GPCRs, and channels. Structural, biochemical, and cellular studies reveal that a sequence motif that defines these ligands binds to a highly conserved interaction surface of the WRC formed by the Sra and Abi subunits. Mutating this binding surface in flies resulted in defects in actin cytoskeletal organization and egg morphology during oogenesis, leading to female sterility. Our findings directly link diverse membrane proteins to the WRC and actin cytoskeleton and have broad physiological and pathological ramifications in metazoans. PubMed: 24439376DOI: 10.1016/j.cell.2013.11.048 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.43 Å) |
Structure validation
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