A multi-angular mass spectrometric view at cyclic nucleotide dependent protein kinases: In vivo characterization and structure/function relationships
✍ Scribed by Arjen Scholten; Thin-Thin Aye; Albert J.R. Heck
- Book ID
- 102943502
- Publisher
- John Wiley and Sons
- Year
- 2008
- Tongue
- English
- Weight
- 768 KB
- Volume
- 27
- Category
- Article
- ISSN
- 0277-7037
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✦ Synopsis
Abstract
Mass spectrometry has evolved in recent years to a well‐accepted and increasingly important complementary technique in molecular and structural biology. Here we review the many contributions mass spectrometry based studies have made in recent years in our understanding of the important cyclic nucleotide activated protein kinase A (PKA) and protein kinase G (PKG). We both describe the characterization of kinase isozymes, substrate phosphorylation, binding partners and post‐translational modifications by proteomics based methodologies as well as their structural and functional properties as revealed by native mass spectrometry, H/D exchange MS and ion mobility. Combining all these mass spectrometry based data with other biophysical and biochemical data has been of great help to unravel the intricate regulation of kinase function in the cell in all its magnificent complexity. © 2008 Wiley Periodicals, Inc. Mass Spec Rev 27: 331–353, 2008