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Phosphorylation and Activation of Myosin by Rho-associated Kinase (Rho-kinase)*
The phosphorylation of MLC by Rho-kinase resulted in the facilitation of the actin activation of myosin ATPase, which may partly account for the mechanism by which Rho regulates cytokinesis, cell motility, or smooth muscle contraction.
Regulation of Myosin Phosphatase by Rho and Rho-Associated Kinase (Rho-Kinase)
Rho appears to inhibit myosin phosphatase through the action of Rho-kinase, which is activated by GTP·RhoA, phosphorylation of MBS and MLC in NIH 3T3 cells.
Small GTP-binding proteins.
In this review, functions of small G proteins and their modes of activation and action are described.
Direct activation of calcium-activated, phospholipid-dependent protein kinase by tumor-promoting phorbol esters.
Rho-Kinase Phosphorylates COOH-terminal Threonines of Ezrin/Radixin/Moesin (ERM) Proteins and Regulates Their Head-to-Tail Association
Observations indicate that the Rho-kinase–dependent phosphorylation interferes with the intramolecular and/ or intermolecular head-to-tail association of ERM proteins, which is an important mechanism of regulation of their activity as actin filament/plasma membrane cross-linkers.
Rho‐associated kinase, a novel serine/threonine kinase, as a putative target for small GTP binding protein Rho.
P purified a Rho‐interacting protein with a molecular mass of approximately 164 kDa (p164) from bovine brain that bound to GTPgammaS (a non‐hydrolyzable GTP analog) and is likely to be a putative target serine/threonine kinase for Rho and serves as a mediator of the RHo‐dependent signaling pathway.
Rac1 and Cdc42 Capture Microtubules through IQGAP1 and CLIP-170
Formation of Actin Stress Fibers and Focal Adhesions Enhanced by Rho-Kinase
Rho-kinase appears to mediate signals from Rho and to induce the formation of stress fibers and focal adhesions.
Rho-Rho-kinase pathway in smooth muscle contraction and cytoskeletal reorganization of non-muscle cells.