Protein arginine methylation: Cellular functions and methods of analysis.
During the last few years, new members of the growing family of protein arginine methyltransferases (PRMTs) have been identified and the role of arginine methylation in manifold cellular processes like signaling, RNA processing, transcription, and subcellular transport has been extensively investigated. In this review, we describe recent methods and findings that have yielded new insights into the cellular functions of arginine-methylated proteins, and we evaluate the currently used procedures for the detection and analysis of arginine methylation.
Pahlich
Steffen
S
Biochemisches Institut, Universität Zürich, Winterthurerstrasse 190, 8057 Zürich, Switzerland.
Zakaryan
Rouzanna P
RP
Gehring
Heinz
H
D001120:Arginine / Q000031:analogs & derivatives / Q000276:immunology / Q000378:metabolism*; D004260:DNA Repair / Q000502:physiology; D044783:F-Box Proteins / Q000378:metabolism; D006801:Humans; D013058:Mass Spectrometry / Q000379:methods; D008780:Methyltransferases / Q000378:metabolism; D011499:Protein Processing, Post-Translational; D011484:Protein-Arginine N-Methyltransferases / Q000378:metabolism*; D040901:Proteomics / Q000379:methods; D012323:RNA Processing, Post-Transcriptional / Q000187:drug effects; D012436:S-Adenosylmethionine / Q000378:metabolism; D015398:Signal Transduction / Q000502:physiology; D014158:Transcription, Genetic / Q000187:drug effects
D044783:F-Box Proteins; C024917:symmetric dimethylarginine; C018524:N,N-dimethylarginine; D012436:S-Adenosylmethionine; D001120:Arginine; D008780:Methyltransferases; C457579:FBXO11 protein, human; C487994:PRMT7 protein, human; D011484:Protein-Arginine N-Methyltransferases