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Arginylation of Beta 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 Kashina 1*
1 Department of Animal Biology, University of Pennsylvania, Philadelphia, PA 19104, USA. 2 The Scripps Research Institute, LaJolla, 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.
Anna Kashina , E-mail: akashina{at}vet.upenn.edu
Posttranslational arginylation is critical for embryogenesis,cardiovascular development, and angiogenesis, but its moleculareffects and the identity of proteins arginylated in vivo areunknown. Here we found that beta actin was arginylated in vivoto regulate actin filament properties, beta actin localization,and lamella formation in motile cells. Arginylation of betaactin apparently represents a critical step in actin N-terminalprocessing needed for actin functioning in vivo. Thus, posttranslationalarginylation of a single protein target can regulate its intracellularfunction, inducing global changes on the cellular level, andmay contribute to cardiovascular development and angiogenesis.
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