title: Control of actin assembly by the WH2 domains and their multifunctional tandem repeats in Spire and Cordon-Bleu.
abstract: The WASP-homology 2 (WH2) domain is a 5-kDa actin-binding protein module that attracts increasing interest by its multifunctional regulation of actin dynamics in motile and morphogenetic processes. Identified by a short consensus sequence LKKT/V originally found in the actin-sequestering ß-thymosin peptides, the ßT/WH2 domains are inserted in a large number of proteins, in particular, the WASP proteins involved in cell protrusions. WH2 are found in tandem repeats in proteins involved in early development and axis-patterning processes, like Spire and Cordon-Bleu. These intrinsically disordered proteins regulate actin assembly in an adaptive and versatile fashion by a fine control of local interaction dynamics within the WH2-actin complex. Versatility is amplified by the protein environment in which the WH2 domain is inserted and by synergy with other adjacent actin-binding modules. Multifunctional activities emerge in WH2 repeats, including filament nucleation, dramatic severing, and barbed end capping or tracking. WH2 domains thus are instrumental in designing customized actin regulators.
authors.affiliation: Cytoskeleton Dynamics and Cell Motility group, CNRS Gif-sur-Yvette, France.
authors.forename: Marie-France
authors.initials: MF
authors.lastname: Carlier
authors.forename: Clotilde
authors.initials: C
authors.lastname: Husson
authors.forename: Louis
authors.initials: L
authors.lastname: Renault
authors.forename: Dominique
authors.initials: D
authors.lastname: Didry
mesh_terms: D000199:Actins / Q000378:metabolism*; D000818:Animals; D006801:Humans; D008840:Microfilament Proteins / Q000737:chemistry* / Q000378:metabolism; D017434:Protein Structure, Tertiary; D051300:Wiskott-Aldrich Syndrome Protein Family / Q000737:chemistry* / Q000378:metabolism*
chemical_list: D000199:Actins; D008840:Microfilament Proteins; D051300:Wiskott-Aldrich Syndrome Protein Family