Arginylation of beta-actin regulates actin cytoskeleton and cell motility. Export

@article{citeulike:1108040, 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.}, address = {Department of Animal Biology, University of Pennsylvania, Philadelphia, PA 19104, USA.}, author = {Karakozova, M. and Kozak, M. and Wong, C. C. and Bailey, A. O. and Yates, J. R. and Mogilner, A. and Zebroski, H. and Kashina, A.}, citeulike-article-id = {1108040}, citeulike-linkout-0 = {http://dx.doi.org/10.1126/science.1129344}, citeulike-linkout-1 = {http://view.ncbi.nlm.nih.gov/pubmed/16794040}, citeulike-linkout-2 = {http://www.hubmed.org/display.cgi?uids=16794040}, day = {14}, doi = {10.1126/science.1129344}, issn = {1095-9203}, journal = {Science}, keywords = {motility}, month = {July}, number = {5784}, pages = {192--196}, posted-at = {2007-02-15 08:11:14}, priority = {2}, title = {Arginylation of beta-actin regulates actin cytoskeleton and cell motility.}, url = {http://dx.doi.org/10.1126/science.1129344}, volume = {313}, year = {2006} }

TY - JOUR ID - citeulike:1108040 L3 - citeulike-article-id:1108040 N2 - 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. IS - 5784 JF - Science SN - 1095-9203 AD - Department of Animal Biology, University of Pennsylvania, Philadelphia, PA 19104, USA. EP - 196 TI - Arginylation of beta-actin regulates actin cytoskeleton and cell motility. VL - 313 SP - 192 KW - motility AU - Karakozova, M AU - Kozak, M AU - Wong, CC AU - Bailey, AO AU - Yates, JR AU - Mogilner, A AU - Zebroski, H AU - Kashina, A PY - 2006/07/14/ UR - http://dx.doi.org/10.1126/science.1129344 ER -