Regulation of transcription factor function by phosphorylation

Citation
Aj. Whitmarsh et Rj. Davis, Regulation of transcription factor function by phosphorylation, CELL MOL L, 57(8-9), 2000, pp. 1172-1183
Citations number
108
Language
INGLESE
art.tipo
Review
Categorie Soggetti
Cell & Developmental Biology
Journal title
CELLULAR AND MOLECULAR LIFE SCIENCES
ISSN journal
1420-682X → ACNP
Volume
57
Issue
8-9
Year of publication
2000
Pages
1172 - 1183
Database
ISI
SICI code
1420-682X(200008)57:8-9<1172:ROTFFB>2.0.ZU;2-P
Abstract
Changes in protein phosphorylation represent a mechanism that is frequently employed by cells to regulate transcription factor activity. In response t o alterations in the extracellular environment, signal transduction pathway s target transcription factors, transcriptional coregulators and chromatin- modifying factors, leading to their phosphorylation by protein kinases or d ephosphorylation by protein phosphatases. These modifications either positi vely or negatively regulate transcription factor activity to facilitate a p rogram of gene expression that results in appropriate changes in cell behav ior. protein phosphorylation and dephosphorylation can directly regulate di stinct aspects of transcription factor function, including cellular localiz ation, protein stability, protein-protein interactions and DNA binding. The phosphorylation-dependent modulation of the activities of transcriptional coregulators and chromatin-modifying factors can also control transcription factor activity. Here we review recent studies that have led to a better u nderstanding of the mechanisms by which protein phosphorylation and dephosp horylation governs transcription factor function.