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J. Biol. Chem., Vol. 278, Issue 29, 27216-27223, July 18, 2003

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p116^Rip Is A Novel Filamentous Actin-binding Protein^*

Jacqueline Mulder , Mieke Poland , Martijn F. B. G. Gebbink  , Jero Calafat ¶, Wouter H. Moolenaar  || and Onno Kranenburg  

From the Division of Cellular Biochemistry and Centre for Biomedical Genetics, and the ^¶Division of Cell Biology, Plesmanlaan 121, The Netherlands Cancer Institute, 1066 CX Amsterdam, The Netherlands

p116^Rip is a ubiquitously expressed protein that was originally identified as a putative binding partner of RhoA in a yeast two-hybrid screen. Overexpression of p116^Rip in neuroblastoma cells inhibits RhoA-mediated cell contraction induced by lysophosphatidic acid (LPA); so far, however, the function of p116^Rip is unknown. Here we report that p116^Rip localizes to filamentous actin (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, p116^Rip is found in the nucleus. Direct interaction or colocalization with RhoA was not detected. We find that p116^Rip binds tightly to F-actin (K_d 0.5 µM) via its N-terminal region, while immunoprecipitation assays show that p116^Rip is complexed to both F-actin and myosin-II. Purified p116^Rip and the F-actin-binding region can bundle F-actin in vitro, as shown by electron microscopy. When overexpressed in NIH3T3 cells, p116^Rip disrupts stress fibers and promotes formation of dendrite-like extensions through its N-terminal actin-binding domain; furthermore, overexpressed p116^Rip inhibits growth factor-induced lamellipodia formation. Our results indicate that p116^Rip is an F-actin-binding protein with in vitro bundling activity and in vivo capability of disassembling the actomyosin-based cytoskeleton.

Received for publication, March 7, 2003 , and in revised form, April 22, 2003.

^* This work was supported by the Dutch Cancer Society. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Present address: University Medical Center Utrecht, 3584 CX Utrecht, The Netherlands.

^|| To whom correspondence should be addressed. Tel.: 31-20-512-1971; Fax: 31-20-512-1989; E-mail: w.moolenaar{at}nki.nl.

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