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Originally published in Science Express on 22 June 2006
Science 14 July 2006:
Vol. 313. no. 5784, pp. 192 - 196
DOI: 10.1126/science.1129344
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Research Articles

Arginylation of ß-Actin Regulates Actin Cytoskeleton and Cell Motility

Marina Karakozova,1 Marina Kozak,1 Catherine C. L. Wong,2 Aaron O. Bailey,2 John R. Yates, III,2 Alexander Mogilner,3 Henry Zebroski,4 Anna Kashina1*

Posttranslational arginylation is critical for mouse embryogenesis, cardiovascular development, and angiogenesis, but its molecular effects and the identity of proteins arginylated in vivo are unknown. We found that ß-actin was arginylated in vivo to regulate actin filament properties, ß-actin localization, and lamella formation in motile cells. Arginylation of ß-actin apparently represents a critical step in the actin N-terminal processing needed for actin functioning in vivo. Thus, posttranslational arginylation of a single protein target can regulate its intracellular function, inducing global changes on the cellular level, and may contribute to cardiovascular development and angiogenesis.

1 Department of Animal Biology, University of Pennsylvania, Philadelphia, PA 19104, USA.
2 The Scripps Research Institute, La Jolla, CA 92037, USA.
3 University of California, Davis, CA 95616, USA.
4 The Rockefeller University, New York, NY 10021, USA.

* To whom correspondence should be addressed. E-mail: akashina{at}vet.upenn.edu

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Science. ISSN 0036-8075 (print), 1095-9203 (online)