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lüll WH2 domain: a small, versatile adapter for actin monomers Paunola E; Mattila PK; Lappalainen PFEBS Lett 2002[Feb]; 513 (1): 92-7The 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.|Actins/chemistry/*metabolism[MESH]|Amino Acid Sequence[MESH]|Animals[MESH]|Binding Sites[MESH]|Cytoskeletal Proteins/chemistry/metabolism[MESH]|Drosophila[MESH]|Drosophila Proteins[MESH]|Humans[MESH]|Microfilament Proteins/chemistry/metabolism[MESH]|Molecular Sequence Data[MESH]|Nerve Tissue Proteins[MESH]|Phylogeny[MESH]|Protein Structure, Secondary[MESH]|Proteins/*chemistry/metabolism[MESH]|Sequence Alignment[MESH]|Sequence Homology, Amino Acid[MESH]|Thymosin/chemistry/metabolism[MESH]|Wiskott-Aldrich Syndrome[MESH]|Wiskott-Aldrich Syndrome Protein[MESH] |