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Sci. STKE, 9 August 2005
Vol. 2005, Issue 296, p. re10
[DOI: 10.1126/stke.2962005re10]

REVIEWS

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

Dave Bridges1 and Greg B. G. Moorhead2*

1Life Sciences Institute, University of Michigan, 210 Washtenaw Avenue, Ann Arbor, MI 48109, USA.
2Department of Biological Sciences, University of Calgary, 2500 University Drive NW, Calgary, AB, Canada 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 2005, re10 (2005).

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