Global discovery of protein kinases and other nucleotide‐binding proteins by mass spectrometry. Issue 5 (5th November 2014)

• Record Type: Journal Article
• Authors: Xiao, Yongsheng; Wang, Yinsheng
• Is Part Of: Mass spectrometry reviews. Volume 35:Issue 5(2016:Sep./Oct.)
• Page Start: 601
• Page End: 619
• Publication Date: 2014-11-05
• Subjects: protein kinases -- kinome -- affinity purification -- protein quantification -- multiple‐reaction monitoring; Mass spectrometry -- Periodicals; 543
• DOI: 10.1002/mas.21447
• Languages: English
• ISSNs: 0277-7037

Abstract

Abstract : Nucleotide‐binding proteins, such as protein kinases, ATPases and GTP‐binding proteins, are among the most important families of proteins that are involved in a number of pivotal cellular processes. However, global study of the structure, function, and expression level of nucleotide‐binding proteins as well as protein–nucleotide interactions can hardly be achieved with the use of conventional approaches owing to enormous diversity of the nucleotide‐binding protein family. Recent advances in mass spectrometry (MS) instrumentation, coupled with a variety of nucleotide‐binding protein enrichment methods, rendered MS‐based proteomics a powerful tool for the comprehensive characterizations of the nucleotide‐binding proteome, especially the kinome. Here, we review the recent developments in the use of mass spectrometry, together with general and widely used affinity enrichment approaches, for the proteome‐wide capture, identification and quantification of nucleotide‐binding proteins, including protein kinases, ATPases, GTPases, and other nucleotide‐binding proteins. The working principles, advantages, and limitations of each enrichment platform in identifying nucleotide‐binding proteins as well as profiling protein–nucleotide interactions are summarized. The perspectives in developing novel MS‐based nucleotide‐binding protein detection platform are also discussed. © 2014 Wiley Periodicals, Inc. Mass Spec Rev 35:601–619, 2016