作者: David W. Litchfield , Brian H. Shilton , Christopher J. Brandl , Laszlo Gyenis
DOI: 10.1016/J.BBAGEN.2015.02.018
关键词:
摘要: Abstract Background Protein phosphorylation is a universal regulatory mechanism that involves an extensive network of protein kinases. The discovery the phosphorylation-dependent peptidyl-prolyl isomerase Pin1 added additional layer complexity to these networks. Scope review We have evaluated interactions between and kinome proline-dependent phosphoproteome taking into consideration findings from targeted studies as well data has emerged systematic phosphoproteomic workflows curated interaction databases. Major conclusions relationship kinase networks not restricted simply recognition proteins are substrates for proline-directed In this respect, itself phosphorylated in cells by kinases modulate its functional properties. Furthermore, targets include number other enzymes such phosphatases subunits actions General significance As result with numerous their substrates, being target phosphorylation, intricate orchestrate complex cellular processes respond environmental cues. This article part Special Issue entitled Proline-directed Foldases: Cell Signaling Catalysts Drug Targets.