Gene interactions and pathways from curated databases and text-mining

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RASA1 — RHOA

Pathways - manually collected, often from reviews:

Text-mined interactions from Literome

Sheffield et al., Acta Crystallogr D Biol Crystallogr 1999 : This GAP activates RhoA and Cdc42Hs, but not Rac
Ellerbroek et al., J Biol Chem 2003 : RhoA phosphorylation or phosphomimetic substitution did not affect Rho guanine nucleotide exchange factor, GTPase activating protein , or geranylgeranyl transferase activity in vitro but promoted binding to the Rho guanine-dissociation inhibitor as measured by exchange factor competition assays
Shang et al., J Biol Chem 2003 : BP-GAP1 selectively enhanced RhoA GTPase activity in vivo although it also interacted strongly with Cdc42 and Rac1
Nakazawa et al., J Neurochem 2008 : In this study, we show that p250GAP , an NMDA receptor associated RhoGAP, regulates spine morphogenesis by modulating RhoA activity
Yang et al., Oncogene 2009 (Neoplasms) : Consistent with this possibility, we found that ectopic overexpression of Ras-GAP in a Ras-GAP-insensitive tumor line impaired the growth suppressing activity of DLC1 and increased RhoA activity in vivo
Bregeon et al., Am J Physiol Cell Physiol 2009 : RhoA activation can result from activation of RhoA exchange factor and/or inhibition of Rho GTPase activating protein ( GAP )
Asnaghi et al., Oncogene 2010 (Carcinoma, Non-Small-Cell Lung...) : The reduction of RhoA activity was dependent on DLC-1 Rho-GAP and p190 Rho-GAP and associated with an increase in a membrane associated p190 Rho-GAP/p120 Ras-GAP complex
Akilesh et al., J Clin Invest 2011 (Glomerulosclerosis, Focal Segmental) : Searching for actin regulatory proteins that are expressed in podocytes, we identified a RhoA activated Rac1 GTPase activating protein ( Rac1-GAP ), Arhgap24, that was upregulated in podocytes as they differentiated, both in vitro and in vivo
Shibata et al., FEBS Lett 1996 : The endogenous and the GAP stimulated GTPase activity of RhoA was inhibited by the interaction with PKN, suggesting the presence of a regulatory mechanism that sustains the GTP bound active form of RhoA