InterProInterPro Protein Domain record

WASH complex, F-actin capping protein, beta subunit
http://metadb.riken.jp/db/SciNetS_rib124i/crib124s1rib124u1698i

WASH complex, F-actin capping protein, beta subunit

InterPro Protein Domain record

description
  • <p>This entry represents a component of the WASH complex. The WASH complex is present at the surface of endosomes and recruits and activates the Arp2/3 complex to induce actin polymerisation. The WASH complex plays a key role in the fission of tubules that serve as transport intermediates during endosome sorting [<cite idref="PUB00054152"/>].</p><p>The WASH complex's subunit structure: F-actin-capping protein subunit alpha (CAPZA1, CAPZA2 or CAPZA3), F-actin-capping protein subunit beta (CAPZB), WASH (WASH1, WASH2P, WASH3P, WASH4P, WASH5P or WASH6P), FAM21 (FAM21A, FAM21B or FAM21C), KIAA1033, KIAA0196 (strumpellin) and CCDC53.</p><p>The actin filament system, a prominent part of the cytoskeleton in eukaryotic cells, is both a static structure and a dynamic network that can undergo rearrangements: it is thought to be involved in processes such as cell movement and phagocytosis [<cite idref="PUB00002626"/>], as well as muscle contraction.</p><p>The F-actin capping protein binds in a calcium-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike gelsolin (see <db_xref db="INTERPRO" dbkey="IPR007122"/>) and severin this protein does not sever actin filaments. The F-actin capping protein is a heterodimer composed of two unrelated subunits: alpha and beta. Neither of the subunits shows sequence similarity to other filament-capping proteins [<cite idref="PUB00002626"/>].</p><p>The beta subunit is a protein of about 280 amino acid residues whose sequence is well conserved in eukaryotic species [<cite idref="PUB00004059"/>].</p>
label
  • WASH complex, F-actin capping protein, beta subunit
attributionURL
signatures_SMART
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contains
PDB_structure
Os_RAPDB_Locus
Pfam-A