RHOA:GTP binds ROCK, activating it

Stable Identifier
Reaction [binding]
Homo sapiens
Locations in the PathwayBrowser
SVG |   | PPTX  | SBGN
Click the image above or here to open this reaction in the Pathway Browser
The layout of this reaction may differ from that in the pathway view due to the constraints in pathway layout

EPHB receptor-induced phosphorylation of coffin is at least partially controlled by Rho-associated kinase (ROCK) and LIM domain kinase (LIMK) activities (Shi et al. 2009). ROCK structure comprises a kinase domain located at the amino terminus of the protein, a coiled-coil region containing the Rho-binding domain (RBD), and a pleckstrin-homology (PH) domain with a cysteine-rich domain (CRD). In resting cells ROCKs exist in an autoinhibition state where the kinase domain interacts with the C-terminal inhibitory region. Binding of active RHOA:GTP to RBD stimulates the phosphotransferase activity of ROCK by disrupting the interaction between the catalytic and the inhibitory C-terminal region of the enzyme (Khalil 2010).

Literature References
PubMed ID Title Journal Year
19553453 Focal adhesion kinase acts downstream of EphB receptors to maintain mature dendritic spines by regulating cofilin activity

Shi, Y, Pontrello, CG, DeFea, KA, Reichardt, LF, Ethell, IM

J. Neurosci. 2009
Participant Of
Orthologous Events
Cite Us!