Rho-associated protein kinase
From Proteopedia
FunctionRho-associated protein kinase (ROCK) is a Rho GTPase effector. ROCK has been shown to regulate cadherin function and thus cell-cell adhesion[1]. ROCKs phosphorylate a large number of actin-binding proteins to modulate their functions. ROCKs are kinases belonging to the AGC (PKA/ PKG/PKC) family of serine-threonine specific protein kinases. DiseaseAberrant ROCK expression and activation contribute to cancer development. ROCK levels are elevated in testicular, bladder and esophageal cancers[2]. RelevanceROCK inhibitors have potential to be developed for treatment of glaucoma and other ocular diseases[3]. Structural highlightsROCK contains several domains including (in ROCK1) a kinase domain (residues 76-338); a coiled-coil region (residues 339-1103) which contains a Rho-binding domain (residues 934-1015) and a pleckstrin homology and cysteine-rich domain (residues 1103-1320) at the C-terminal. making interactions with a [4]. 3D structures of Rho-associated protein kinaseRho-associated protein kinase 3D structures References
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