Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.
STEM Talent Event

Site Tools

  • AAAS
  • Subscribe
  • Feedback

Site Search

Search Advanced

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).

Read the Full Text

THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
RIM1{alpha} phosphorylation at serine-413 by protein kinase A is not required for presynaptic long-term plasticity or learning.
P. S. Kaeser, H.-B. Kwon, J. Blundell, V. Chevaleyre, W. Morishita, R. C. Malenka, C. M. Powell, P. E. Castillo, and T. C. Sudhof (2008)
PNAS 105, 14680-14685
   Abstract »    Full Text »    PDF »
Regulation of Nuclear Import/Export of Carbohydrate Response Element-binding Protein (ChREBP): INTERACTION OF AN {alpha}-HELIX OF ChREBP WITH THE 14-3-3 PROTEINS AND REGULATION BY PHOSPHORYLATION.
H. Sakiyama, R. M. Wynn, W.-R. Lee, M. Fukasawa, H. Mizuguchi, K. H. Gardner, J. J. Repa, and K. Uyeda (2008)
J. Biol. Chem. 283, 24899-24908
   Abstract »    Full Text »    PDF »
Phospho-specific binding of 14-3-3 proteins to phosphatidylinositol 4-kinase III {beta} protects from dephosphorylation and stabilizes lipid kinase activity.
A. Hausser, G. Link, M. Hoene, C. Russo, O. Selchow, and K. Pfizenmaier (2006)
J. Cell Sci. 119, 3613-3621
   Abstract »    Full Text »    PDF »
Glucose Signaling in Saccharomyces cerevisiae.
G. M. Santangelo (2006)
Microbiol. Mol. Biol. Rev. 70, 253-282
   Abstract »    Full Text »    PDF »
Structure/Function Analysis of Tristetraprolin (TTP): p38 Stress-Activated Protein Kinase and Lipopolysaccharide Stimulation Do Not Alter TTP Function.
W. F. C. Rigby, K. Roy, J. Collins, S. Rigby, J. E. Connolly, D. B. Bloch, and S. A. Brooks (2005)
J. Immunol. 174, 7883-7893
   Abstract »    Full Text »    PDF »
Selecton: a server for detecting evolutionary forces at a single amino-acid site.
A. Doron-Faigenboim, A. Stern, I. Mayrose, E. Bacharach, and T. Pupko (2005)
Bioinformatics 21, 2101-2103
   Abstract »    Full Text »    PDF »

ADVERTISEMENT
Click Me!

ADVERTISEMENT
Click Me!

To Advertise     Find Products

Science Signaling. ISSN 1937-9145 (pre-2008: Science's STKE. ISSN 1525-8882)