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Reference Report
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| Citation | Paunola, E., Mattila, P.K., Lappalainen, P. (2002). WH2 domain: a small, versatile adapter for actin monomers. FEBS Lett. 513(1): 92--97. (Export to RIS) | ||
| FlyBase ID | FBrf0147028 | ||
| Publication Type | Review | ||
| PubMed ID | 11911886 | ||
| PubMed Abstract | The actin cytoskeleton plays a central role in many cell biological processes. The structure and dynamics of the actin cytoskeleton are regulated by numerous actin-binding proteins that usually contain one of the few known actin-binding motifs. WH2 domain (WASP homology domain-2) is a approximately 35 residue actin monomer-binding motif, that is found in many different regulators of the actin cytoskeleton, including the beta-thymosins, ciboulot, WASP (Wiskott Aldrich syndrome protein), verprolin/WIP (WASP-interacting protein), Srv2/CAP (adenylyl cyclase-associated protein) and several uncharacterized proteins. The most highly conserved residues in the WH2 domain are important in beta-thymosin's interactions with actin monomers, suggesting that all WH2 domains may interact with actin monomers through similar interfaces. Our sequence database searches did not reveal any WH2 domain-containing proteins in plants. However, we found three classes of these proteins: WASP, Srv2/CAP and verprolin/WIP in yeast and animals. This suggests that the WH2 domain is an ancient actin monomer-binding motif that existed before the divergence of fungal and animal lineages. | ||
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| Language of Publication | English | ||
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| Publication Type | Journal | ||
| Abbreviation | FEBS Lett. | ||
| Title | FEBS Letters | ||
| Publication Year | 1968- | ||
| ISBN/ISSN | 0014-5793 | ||
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Data from Reference
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| Genes (7)
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