The Intricacies of P21 Phosphorylation: Protein/Protein Interactions, Subcellular Localization and Stability.
From: Division of Cell & Molecular Biology, Faculty of Natural Sciences, Imperial College London, South Kensington, London, UK. emma.child@imperial.ac.uk
Cell cycle (Georgetown, Tex.)
- Publish Date: Jun 2006
- ISSN: 1551-4005
- Volume: 5
- Issue: 12
- Pages: 1313-9
- Medium: Internet
- Language: English
- Citation (JAMA): Child Emma S, Mann David J, et al. The Intricacies of P21 Phosphorylation: Protein/Protein Interactions, Subcellular Localization and Stability.. Cell Cycle Jun 2006;5:1313-9
Abstract
p21 was originally described as functioning as a cell cycle regulator via inhibition of both cyclin-dependent kinases and processive DNA replication. Nowadays it is recognized to play other fundamental roles including transcriptional regulation and the modulation of apoptosis. Each of these functions of p21 is achieved through direct p21/protein interactions and the subcellular localization of p21 plays an important part in dictating the binding partners to which p21 is exposed. Over recent years, a number of phosphorylation sites in p21 have been identified, these being targeted by several important intracellular signalling protein kinases. Here we review the state of our knowledge of p21 phosphorylation with respect to the kinases involved and the molecular biological effects of each phosphorylation event.
Mesh Headings (Keywords): Animals, Cyclin-Dependent Kinase Inhibitor p21, Humans, Phosphorylation, Phosphoserine, Phosphothreonine, Protein Binding
Check for Full Text / PubMed Unique Identifier (PMID): 16775416
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