Publication Date:
2006-06-24
Description:
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.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Karakozova, Marina -- Kozak, Marina -- Wong, Catherine C L -- Bailey, Aaron O -- Yates, John R 3rd -- Mogilner, Alexander -- Zebroski, Henry -- Kashina, Anna -- P41 RR11823-09/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 2006 Jul 14;313(5784):192-6. Epub 2006 Jun 22.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Animal Biology, University of Pennsylvania, Philadelphia, PA 19104, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16794040" target="_blank"〉PubMed〈/a〉
Keywords:
Actin Cytoskeleton/*metabolism/ultrastructure
;
Actins/chemistry/*metabolism
;
Aminoacyltransferases/genetics/metabolism
;
Animals
;
Arginine/chemistry/*metabolism
;
*Cell Movement
;
Cell Shape
;
Cell Size
;
Fibroblasts
;
Immunoprecipitation
;
Isoelectric Point
;
Mass Spectrometry
;
Mice
;
Protein Binding
;
Protein Isoforms/chemistry/metabolism
;
Pseudopodia/metabolism/ultrastructure
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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