Comprehending dynamic protein methylation with mass spectrometry

Leila Afjehi-Sadat, Benjamin A. Garcia

Research output: Contribution to journalReview articlepeer-review

39 Scopus citations

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.

Original languageEnglish
Pages (from-to)12-19
Number of pages8
JournalCurrent Opinion in Chemical Biology
Volume17
Issue number1
DOIs
StatePublished - Feb 2013

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