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Sci. STKE, 20 July 2004
Vol. 2004, Issue 242, p. re10
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.
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.