Rabbit polyclonal antibody to M~RIP

Myosin phosphatase~rho interacting protein (M~RIP), also known as p116RIP, RIP3, and MPRIP, localizes to actin~myosin filaments regulating cytoskeletal dynamics. M~RIP contains amino~terminal pleckstrin homology domains, carboxyl~terminal coiled~coil domains, and was originally identified to associate with the myosin phosphatase complex. M~RIP binds to MBS/MYRT, the myosin binding subunit of myosin phosphatase, as well as RhoA. Phosphorylation of MYRT by Rho~associated kinase (ROCK) inhibits myosin phosphatase activity, resulting in increased levels of phosphorylation on myosin light chain, and enhanced contractility. M~RIP may function as a scaffolding protein for the complex between the myosin phosphatase complex, Rho/ROCK, and actin. Silencing of M~RIP results in disassembly of the complex, increased phosphorylation of myosin light chain, and changes to cytoskeletal dynamics.