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Details on Person EPHB receptor-induced phosphorylation of coffin is at least ...
| Class:Id | Summation:3928273 |
|---|---|
| _displayName | EPHB receptor-induced phosphorylation of coffin is at least ... |
| _timestamp | 2013-10-03 09:45:38 |
| created | [InstanceEdit:3928288] Garapati, P V, 2013-07-22 |
| literatureReference | [URL:4640882] http://www.ncbi.nlm.nih.gov/books/NBK54588/ |
| modified | [InstanceEdit:4640880] Garapati, P V, 2013-09-27 [InstanceEdit:4655453] Garapati, P V, 2013-10-03 |
| text | 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). |
| (summation) | [Reaction:3928576] RHOA:GTP binds ROCK, activating it [Homo sapiens] |
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No pathways have been reviewed or authored by EPHB receptor-induced phosphorylation of coffin is at least ... (3928273)
