14-3-3 proteins: regulation of subcellular localization by molecular interference |
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Authors: | Muslin A J Xing H |
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Institution: | Center for Cardiovascular Research, Department of Medicine, School of Medicine, Washington University, Box 8086 - Cardiology, 660 South Euclid Avenue, 63110, St. Louis, MO, USA. amuslin@im.wustl.edu |
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Abstract: | 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). In 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. |
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Keywords: | 14-3-3 Protein Signal transduction Apoptosis Cell cycle Phosphoserine Protein– protein interaction Nuclear import Nuclear export |
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