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Details on Person ROCK proteins are thought to be autoinhibited by interaction...
| Class:Id | Summation:5229007 |
|---|---|
| _displayName | ROCK proteins are thought to be autoinhibited by interaction... |
| _timestamp | 2014-01-15 10:25:22 |
| created | [InstanceEdit:5229005] Garapati, P V, 2014-01-15 |
| literatureReference | [LiteratureReference:3927978] Rho-associated coiled-coil-forming kinases (ROCKs): potential targets for the treatment of atherosclerosis and vascular disease [LiteratureReference:3927998] Regulation and functions of Rho-associated kinase [LiteratureReference:421378] The small GTP-binding protein Rho binds to and activates a 160 kDa Ser/Thr protein kinase homologous to myotonic dystrophy kinase [LiteratureReference:5229002] Crystal structure of a coiled-coil domain from human ROCK I |
| text | ROCK proteins are thought to be autoinhibited by interactions between the N-terminal kinase domain and the C-terminal Rho binding domain (RBD) and pleckstrin homology (PH) domains. Interaction between RHOA-GTP and the RBD disrupts ROCK's autoinhibition by suppressing the carboxyl-terminal RBD-PH domain on the amino-terminal kinase domain, leading to an active open kinase domain. ROCKs mediate Rho-induced actin cytoskeletal changes through effects on myosin light chain (MLC) phosphorylation (Zhou et al. 2011, Amano et al. 2000, Tu et al. 2011). |
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