title: Comprehending dynamic protein methylation with mass spectrometry.
abstract: Protein methylation is a post-translational modification (PTM) which modulates cellular and biological processes including transcription, RNA processing, protein interactions and protein dynamics. Methylation, catalyzed by highly specific methyltransferase enzymes, occurs on several amino acids including arginine, lysine, histidine and dicarboxylic amino acids like glutamate. Mass spectrometry (MS)-based techniques continue to be the methods of choice for the study of protein PTMs. These approaches are powerful and sensitive tools that have been used to identify, quantify and characterize protein methylation. In addition, metabolic labeling strategies can be coupled to MS detection in order to measure dynamic and differential in vivo protein methylation rates. In this review, different applications of mass spectrometry technologies and methods to study protein methylation are discussed.
authors: Epigenetics Program, Perelman School of Medicine, University of Pennsylvania, 1009C Stellar-Chance Laboratories, 422 Curie Boulevard, Philadelphia, PA 19104, USA.
authors: Leila
authors: L
authors: Afjehi-Sadat
authors: Benjamin A
authors: BA
authors: Garcia
mesh_terms: D000596:Amino Acids / Q000032:analysis / Q000378:metabolism; D000818:Animals; D006657:Histones / Q000737:chemistry / Q000378:metabolism; D006801:Humans; D013058:Mass Spectrometry / Q000295:instrumentation / Q000379:methods*; D008745:Methylation; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism
chemical_list: D000596:Amino Acids; D006657:Histones; D011506:Proteins