ARHGAP10
Domain
The BAR domain is important to associate RAB8A (or RAB8B) and RAB10 to endosomal membrane to promote tubule extension. The BAR domain is also important to recruit WDR44 to endosomal tubules.
Function
GTPase-activating protein that catalyzes the conversion of active GTP-bound Rho GTPases to their inactive GDP-bound form, thus suppressing various Rho GTPase-mediated cellular processes (PubMed:11432776). Also converts Cdc42 to an inactive GDP-bound state (PubMed:11432776). Essential for PTKB2 regulation of cytoskeletal organization via Rho family GTPases. Inhibits PAK2 proteolytic fragment PAK-2p34 kinase activity and changes its localization from the nucleus to the perinuclear region. Stabilizes PAK-2p34 thereby increasing stimulation of cell death (By similarity). Associates with MICAL1 on the endosomal membrane to promote Rab8-Rab10-dependent tubule extension. After dissociation with MICAL1, recruits WDR44 which connects the endoplasmic reticulum (ER) with the endosomal tubule, thereby participating in the export of a subset of neosynthesized proteins (PubMed:32344433).
Post-translational modifications
Phosphorylated. Phosphorylated in vitro by constitutive active PKN3.
Tissue Specificity
High levels of expression in heart and skeletal muscle.
Cellular localization
- Cytoplasm
- Cytoplasm
- Perinuclear region
- Cell membrane
- Endosome membrane
- Association to cell membrane is dependent on PH domain. Colocalized with MICAL1, RAB8A, RAB8B and RAB10 on endosomal tubules (PubMed:32344433).
Alternative names
GRAF2, ARHGAP10, Rho GTPase-activating protein 10, GTPase regulator associated with focal adhesion kinase 2, Graf-related protein 2, Rho-type GTPase-activating protein 10