WH2 domain: a small, versatile adapter for actin monomers
: Paunola E, Mattila PK, Lappalainen P
Publisher: ELSEVIER SCIENCE BV
: 2002
FEBS Letters
: FEBS LETTERS
: FEBS LETT
: PII S0014-5793(01)03242-2
: 513
: 1
: 92
: 97
: 6
: 0014-5793
DOI: https://doi.org/10.1016/S0014-5793(01)03242-2
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 similar to35 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. (C) 2002 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.
actin, beta-thymosin, verprolin, Wiskott Aldrich syndrome protein homology domain-2
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