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MBC in Press, published online ahead of print October 6, 2004
Mol. Biol. Cell 10.1091/mbc.E04-04-0275

A more recent version of this article appeared on December 1, 2004
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Submitted on April 1, 2004
Revised on September 17, 2004
Accepted on September 23, 2004

p116Rip Targets Myosin Phosphatase to the Actin Cytoskeleton and Is Essential for RhoA/ROCK-regulated Neuritogenesis

Jacqueline Mulder, Aafke Ariaens, Dick van den Boomen, and Wouter H. Moolenaar*

Division of Cellular Biochemistry and Centre for Biomedical Genetics, The Netherlands Cancer Institute, 1066 CX Amsterdam, The Netherlands

Monitoring Editor: Anne Ridley

Activation of the RhoA-Rho kinase (ROCK) pathway stimulates actomyosin-driven contractility in many cell systems, largely through ROCK-mediated inhibition of myosin-II light-chain phosphatase. In neuronal cells, the RhoA-ROCK-actomyosin pathway signals cell rounding, growth cone collapse and neurite retraction; conversely, inhibition of RhoA/ROCK promotes cell spreading and neurite outgrowth. The actin-binding protein p116Rip, whose N-terminal region bundles F-actin in vitro, has been implicated in Rho-dependent neurite remodeling; however, its function is largely unknown. Here we show that p116Rip, through its C-terminal coiled-coil domain, interacts directly with the C-terminal leucine zipper of the regulatory myosin-binding subunits of myosin-II phosphatase, MBS85 and MBS130. RNAi-induced knockdown of p116Rip inhibits cell spreading and neurite outgrowth in response to extracellular cues, without interfering with the regulation of myosin light-chain phosphorylation. We conclude that p116Rip is essential for neurite outgrowth and may act as a scaffold to target the myosin phosphatase complex to the actin cytoskeleton.

*Corresponding author. E-mail: w.moolenaar{at}nki.nl






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