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Papers In Press, published online ahead of print May 5, 2003
Cellular Biochemistry, The Netherlands Cancer Institute, Amsterdam 1066 CX
Corresponding Author: w.moolenaar{at}nki.nl
p116Rip is a ubiquitously expressed protein that was originally identified as a putative binding partner of RhoA in a yeast two-hybrid screen. Overexpression of p116Rip in neuroblastoma cells inhibits RhoA-mediated cell contraction induced by lysophosphatidic acid (LPA), but to date the function of p116Rip is unknown. Here we report that p116Rip localizes to F-actin-rich structures, including stress fibers and cortical microfilaments, in both serum-deprived and LPA-stimulated cells, with the N-terminus (residues 1-382) dictating cytoskeletal localization. In addition, p116Rip is found in the nucleus. Direct interaction or colocalization with RhoA was not detected. We find that p116Rip binds tightly to F-actin (Kd ~ 0.5 mM) via its N-terminal region, whilst immunoprecipitation assays show that p116Rip is complexed to both F-actin and myosin-II. Purified p116Rip and the F-actin-binding region can bundle F-actin in vitro, as shown by electron microscopy. When overexpressed in NIH3T3 cells, p116Rip disrupts stress fibers and promotes formation of dendrite-like extensions through its N-terminal actin-binding domain; furthermore, overexpressed p116Rip inhibits growth factor-induced lamellipodia formation. Our results indicate that p116Rip is an F-actin-binding protein with in vitro bundling activity and in vivo capability of disassembling the actomyosin-based cytoskeleton.
J. Biol. Chem, 10.1074/jbc.M302399200
Submitted on March 7, 2003
Revised on April 22, 2003
Accepted on May 4, 2003
p116Rip is a novel F-actin-binding protein
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