SH3 domain-binding protein 1

Definition:

GTPase activating protein (GAP) which specifically converts GTP-bound Rho-type GTPases including RAC1 and CDC42 in their inactive GDP-bound form. By specifically inactivating RAC1 at the leading edge of migrating cells, it regulates the spatiotemporal organization of cell protrusions which is important for proper cell migration. Also negatively regulates CDC42 in the process of actin remodeling and the formation of epithelial cell junctions. Through its GAP activity toward RAC1 and/or CDC42 plays a specific role in phagocytosis of large particles. Specifically recruited by a PI3 kinase/PI3K-dependent mechanism to sites of large particles engagement, inactivates RAC1 and/or CDC42 allowing the reorganization of the underlying actin cytoskeleton required for engulfment. It also plays a role in angiogenesis and the process of repulsive guidance as part of a semaphorin-plexin signaling pathway. Following the binding of PLXND1 to extracellular SEMA3E it dissociates from PLXND1 and inactivates RAC1, inducing the intracellular reorganization of the actin cytoskeleton and the collapse of cells.

References:

[1]. Maria Carla Parrini, et al. SH3BP1, an exocyst-associated RhoGAP, inactivates Rac1 at the front to drive cell motility. Mol Cell. 2011 Jun 10;42(5):650-61. [Content Brief]

[2]. Ahmed Elbediwy, et al. Epithelial junction formation requires confinement of Cdc42 activity by a novel SH3BP1 complex. J Cell Biol. 2012 Aug 20;198(4):677-93. [Content Brief]

[3]. Aleksandra Tata, et al. An image-based RNAi screen identifies SH3BP1 as a key effector of Semaphorin 3E-PlexinD1 signaling. J Cell Biol. 2014 May 26;205(4):573-90. [Content Brief]

[4]. Daniel Schlam, et al. Phosphoinositide 3-kinase enables phagocytosis of large particles by terminating actin assembly through Rac/Cdc42 GTPase-activating proteins. Nat Commun. 2015 Oct 14;6:8623. [Content Brief]

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