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Biochemical Journal logoLink to Biochemical Journal
. 2004 Apr 15;379(Pt 2):e1–e2. doi: 10.1042/BJ20040284

Master of all things phosphorylated.

Michael B Yaffe 1
PMCID: PMC1224097  PMID: 15061704

Abstract

Serine/threonine phosphorylation plays a central role in cellular regulation, either by altering a protein's activity directly or by inducing specific protein-protein interactions, which, in turn, affect localization, binding specificity or activity. One group of molecules that bind to phosphoserine/phosphothreonine-containing sequences are the 14-3-3 proteins, which regulate a wide range of cellular targets. A new analysis of the 14-3-3 phosphoproteome using affinity chromatography has revealed many previously unknown 14-3-3 ligands whose binding to 14-3-3 proteins is phosphorylation-dependent. This study paves the way for future work on these important 14-3-3-interacting proteins.


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