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• W2337226471 endingPage "92" @default.
• W2337226471 startingPage "82" @default.
• W2337226471 abstract "The Rho-associated coiled-coil containing kinases (ROCK) were first identified as effectors of the small GTPase RhoA, hence their nomenclature. Since their discovery, two decades ago, scientists have sought to unravel the structure, regulation, and function of these essential kinases. During that time, a consensus model has formed, in which ROCK activity is regulated via both Rho-dependent and independent mechanisms. However, recent findings have raised significant questions regarding this model. In their recent publication in Nature Communications, Truebestein and colleagues present the structure of a full-length Rho kinase for the first time. In contrast to previous reports, the authors could find no evidence for autoinhibition, RhoA binding, or regulation of kinase activity by phosphorylation. Instead, they propose that ROCK functions as a molecular ruler, in which the central coiled-coil bridges the membrane-binding regulatory domains to the kinase domains at a fixed distance from the plasma membrane. Here, we explore the consequences of the new findings, re-examine old data in the context of this model, and emphasize outstanding questions in the field." @default.
• W2337226471 created "2016-06-24" @default.
• W2337226471 creator A5048866718 @default.
• W2337226471 creator A5065287638 @default.
• W2337226471 creator A5081592343 @default.
• W2337226471 date "2016-04-02" @default.
• W2337226471 modified "2023-10-10" @default.
• W2337226471 title "Made to measure – keeping Rho kinase at a distance" @default.
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• W2337226471 doi "https://doi.org/10.1080/21541248.2016.1173770" @default.
• W2337226471 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4905274" @default.
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