Arginylation of beta-actin regulates actin cytoskeleton and cell motility.
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.
Karakozova
Marina
M
Department of Animal Biology, University of Pennsylvania, Philadelphia, PA 19104, USA.
Kozak
Marina
M
Wong
Catherine C L
CC
Bailey
Aaron O
AO
Yates
John R
JR
Mogilner
Alexander
A
Zebroski
Henry
H
Kashina
Anna
A
D008841:Actin Cytoskeleton / Q000378:metabolism* / Q000648:ultrastructure; D000199:Actins / Q000737:chemistry / Q000378:metabolism*; D019881:Aminoacyltransferases / Q000235:genetics / Q000378:metabolism; D000818:Animals; D001120:Arginine / Q000737:chemistry / Q000378:metabolism*; D002465:Cell Movement; D048430:Cell Shape; D048429:Cell Size; D005347:Fibroblasts; D047468:Immunoprecipitation; D007526:Isoelectric Point; D013058:Mass Spectrometry; D051379:Mice; D011485:Protein Binding; D020033:Protein Isoforms / Q000737:chemistry / Q000378:metabolism; D011554:Pseudopodia / Q000378:metabolism / Q000648:ultrastructure
D000199:Actins; D020033:Protein Isoforms; D001120:Arginine; D019881:Aminoacyltransferases; C019727:arginyltransferase