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Sci. STKE, 20 July 2004
Vol. 2004, Issue 242, p. re10
[DOI: 10.1126/stke.2422004re10]

REVIEWS

14-3-3 Proteins: A Number of Functions for a Numbered Protein

Dave Bridges1 and Greg B. G. Moorhead1*

1Department of Biological Sciences, University of Calgary, 2500 University Drive N.W., Calgary, Canada AB T2N 1N4.

Abstract: Many signal transduction events are orchestrated by specific interactions of proteins mediated through discrete phosphopeptide-binding motifs. Although several phosphospecific-binding domains are now known, 14-3-3s were the first proteins recognized to specifically bind a discrete phosphoserine or phosphothreonine motif. The 14-3-3 proteins are a family of ubiquitously expressed, exclusively eukaryotic proteins with an astonishingly large number of binding partners. Consequently, 14-3-3s modulate an enormous and diverse group of cellular processes. The effects of 14-3-3 proteins on their targets can be broadly defined using three categories: (i) conformational change; (ii) physical occlusion of sequence-specific or structural protein features; and (iii) scaffolding. This review will describe the current state of knowledge on 14-3-3 proteins, highlighting several important advances, and will attempt to provide a framework by which 14-3-3 functions can be understood.

*Corresponding author. Fax: 403-289-9311, e-mail: Moorhead{at}ucalgary.ca.

Citation: D. Bridges, G. B. G. Moorhead, 14-3-3 Proteins: A Number of Functions for a Numbered Protein. Sci. STKE 2004, re10 (2004).

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