DIAPH1 binds RHOA:GTP

Stable Identifier
R-HSA-5665989
Type
Reaction
Species
Homo sapiens
Compartment
Locations in the PathwayBrowser
Summation

DIAPH1 is activated by binding of the DIAPH1 dimer to GTP-bound (active) RHOA. Binding to RHOA releaves the autoinhibitory interaction of DIAPH1 FH3 and DAD domains (Otomo et al. 2005). Phosphorylation of RHOA at serine residue S188 may be required for RHOA binding to DIAPH1 (Li and Sewer 2010). The interaction between RHOA and DIAPH1 may also be positively regulated by PI3K signaling (Gao et al. 2009).

Literature References
PubMed ID Title Journal Year
20591975 RhoA and DIAPH1 mediate adrenocorticotropin-stimulated cortisol biosynthesis by regulating mitochondrial trafficking

Li, D, Sewer, MB

Endocrinology 2010
20030946 [PI3-kinase mediates activity of RhoA and interaction of RhoA with mDia1 in thrombin-induced platelet aggregation]

Gao, GX, Dong, HJ, Gu, HT, Gao, Y, Pan, YZ, Yang, Y, Chen, XQ

Zhongguo Shi Yan Xue Ye Xue Za Zhi 2009
15866170 Structural basis of Rho GTPase-mediated activation of the formin mDia1

Otomo, T, Otomo, C, Tomchick, DR, Machius, M, Rosen, MK

Mol. Cell 2005
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