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Arginylation of ß-Actin Regulates Actin Cytoskeleton and Cell Motility
Marina Karakozova,1Marina Kozak,1Catherine C. L. Wong,2Aaron O. Bailey,2John R. Yates, III,2Alexander Mogilner,3Henry Zebroski,4Anna Kashina1*
Posttranslational arginylation is critical for mouse embryogenesis,cardiovascular development, and angiogenesis, but its moleculareffects and the identity of proteins arginylated in vivo areunknown. We found that ß-actin was arginylated invivo to regulate actin filament properties, ß-actinlocalization, and lamella formation in motile cells. Arginylationof ß-actin apparently represents a critical step inthe actin N-terminal processing needed for actin functioningin vivo. Thus, posttranslational arginylation of a single proteintarget can regulate its intracellular function, inducing globalchanges on the cellular level, and may contribute to cardiovasculardevelopment 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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