Journal
CELLULAR SIGNALLING
Volume 12, Issue 11-12, Pages 703-709Publisher
ELSEVIER SCIENCE INC
DOI: 10.1016/S0898-6568(00)00131-5
Keywords
14-3-3 protein; signal transduction; apoptosis; cell cycle; phosphoserine; protein-protein interaction; nuclear import; nuclear export
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Funding
- NIGMS NIH HHS [GM 54620] Funding Source: Medline
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The 14-3-3 family of proteins plays a key regulatory role in signal transduction, checkpoint control, apoptotic, and nutrient-sensing pathways. 14-3-3 proteins act by binding to partner proteins, and this binding often leads to the altered subcellular localization of the partner. 14-3-3 proteins promote the cytoplasmic localization of many binding partners, including the pro-apoptotic protein BAD and the cell cycle regulatory phosphatase Cdc25C, but they can also promote the nuclear localization of other partners, such as the catalytic subunit of telomerase (TERT). Ln some cases, 14-3-3 binding has no effect on the subcellular localization of a partner. 14-3-3 may affect the localization of a protein by interfering with the function of a nearby targeting sequence, such as a nuclear localization sequence (NLS) or a nuclear export sequence (NES), on the binding partner. (C) 2000 Elsevier Science Inc. All rights reserved.
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