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The protein encoded by ARAP2 contains ARF-GAP, RHO-GAP, ankyrin repeat, RAS-associating, and pleckstrin homology domains.
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These results highlight an Arf GAP-independent function of ARAP2 in regulating Akt activity.
ACAP1 and ARAP2 each colocalize with Arf6 but they did not colocalize with each other and have opposing effects on focal adhesions.
ARAP2 signals through Arf6 and Rac1 to control focal adhesion morphology
Our findings indicate that ARAP2 promotes InlB-mediated entry of Listeria monocytogenes in part, by antagonizing the host GTPase Arf6.
ARAP2 is an Arf6GAP that functions downstream of RhoA to regulate focal adhesion dynamics.
ARAP2 knockdown did not affect fatty acid uptake but reduced basal glucose uptake, total levels of the glucose transporter GLUT1, and GLUT1 levels in the plasma membrane and the lipid micro-domain fraction.
The protein encoded by this gene contains ARF-GAP, RHO-GAP, ankyrin repeat, RAS-associating, and pleckstrin homology domains. The protein is a phosphatidylinositol (3,4,5)-trisphosphate-dependent Arf6 GAP that binds RhoA-GTP, but it lacks the predicted catalytic arginine in the RHO-GAP domain and does not have RHO-GAP activity. The protein associates with focal adhesions and functions downstream of RhoA to regulate focal adhesion dynamics.
Arf and Rho GAP adapter protein 2
, arf-GAP with Rho-GAP domain, ANK repeat and PH domain-containing protein 2
, centaurin, delta 1
, PARX protein
, centaurin delta 1
, ArfGAP with RhoGAP domain, ankyrin repeat and PH domain 2
, arf-GAP with Rho-GAP domain, ANK repeat and PH domain-containing protein 2-like