Arginylation of beta-actin regulates actin cytoskeleton and cell motility |
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Authors: | Karakozova Marina Kozak Marina Wong Catherine C L Bailey Aaron O Yates John R Mogilner Alexander Zebroski Henry Kashina Anna |
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Institution: | Department of Animal Biology, University of Pennsylvania, Philadelphia, PA 19104, USA. |
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Abstract: | 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 beta-actin was arginylated in vivo to regulate actin filament properties, beta-actin localization, and lamella formation in motile cells. Arginylation of beta-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. |
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