Zurück zu Ihrem Suchergebnis

Beschreibung

Switch-associated protein 70 (UniProt: Q9UH65, also known as SWAP-70) is encoded by the SWAP70 (also known as KIAA0640, HSPC321) gene (Gene ID: 23075) in human. SWAP-70 is a phosphatidylinositol 3,4,5-trisphosphate (PIP3)-dependent guanine nucleotide exchange factor (GEF) that, independently of RAS, transduces signals from tyrosine kinase receptors to RAC. SWAP-70 regulates the actin cytoskeleton as an effector or adapter protein in response to agonist stimulated phosphatidylinositol (3,4)-bisphosphate production and cell protrusion. It is expressed only in mature B-cells including those associated with mucosa-associated tissue and bronchus-associated tissue. In resting B-cells it is localized mainly in the cytoplasm and upon cell activation it is recruited to the plasma membrane and then translocates to the nucleus. In activated, class-switching B-cells it is associated with membrane IgG, but not IgM. It is also widely expressed in spleen, kidney, lung, and liver. SWAP-70 has an N-terminal putative EF-hand domain, a pleckstrin homology (PH) domain (aa 210-306) that binds phosphatidylinositol 3,4,5-trisphosphate and is responsible for membrane localization, a tri-partite coiled-coil region (aa 316-539), and a C-terminal F-actin-binding site through which it specifically binds non-muscle actin. (Ref.: Chacó,n-Martí,nez, CA et al. (2103). J. Biol. Chem. 288(40), 28687-28703).