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

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

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

  1. Dave Bridges1 and
  2. Greg B. G. Moorhead1,*
  1. 1Department of Biological Sciences, University of Calgary, 2500 University Drive N.W., Calgary, Canada AB T2N 1N4.
  1. *Corresponding author. Fax: 403-289-9311, e-mail: Moorhead{at}ucalgary.ca.

Gloss

Signal transduction events can be regulated both by posttranslational modifications and by protein-protein interactions. 14-3-3 proteins are critically involved in both of these processes. The 14-3-3s, originally catalogued as small, abundant brain proteins, are expressed as multiple isoforms in all eukaryotic cells and are now known to recognize and to bind to distinct phosphoserine or phosphothreonine motifs on target proteins. Their binding partners include key proteins involved in metabolism, cell cycle control, the DNA damage response, transcription, protein synthesis, and apoptosis. This STKE Review with 2 figures, 1 interactive molecular structure, and 118 references describes 14-3-3 proteins and highlights how these simple proteins have profound effects on the regulation of a vast number of cellular events.

Citation:

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

A Proteome-wide Domain-centric Perspective on Protein Phosphorylation
A. Palmeri, G. Ausiello, F. Ferre, M. Helmer-Citterich, and P. F. Gherardini
MCP 13, 2198-2212 (1 September 2014)

Parkinson-related LRRK2 mutation R1441C/G/H impairs PKA phosphorylation of LRRK2 and disrupts its interaction with 14-3-3
K. Muda, D. Bertinetti, F. Gesellchen, J. S. Hermann, F. von Zweydorf, A. Geerlof, A. Jacob, M. Ueffing, C. J. Gloeckner, F. W. Herberg et al.
Proc. Natl. Acad. Sci. USA 111, E34-E43 (7 January 2014)

Structural Basis for the 14-3-3 Protein-dependent Inhibition of the Regulator of G Protein Signaling 3 (RGS3) Function
L. Rezabkova, P. Man, P. Novak, P. Herman, J. Vecer, V. Obsilova, and T. Obsil
J Biol Chem 286, 43527-43536 (16 December 2011)

FoxO6 Integrates Insulin Signaling With Gluconeogenesis in the Liver
D. H. Kim, G. Perdomo, T. Zhang, S. Slusher, S. Lee, B. E. Phillips, Y. Fan, N. Giannoukakis, R. Gramignoli, S. Strom et al.
Diabetes 60, 2763-2774 (1 November 2011)

14-3-3 Protein Masks the DNA Binding Interface of Forkhead Transcription Factor FOXO4
J. Silhan, P. Vacha, P. Strnadova, J. Vecer, P. Herman, M. Sulc, J. Teisinger, V. Obsilova, and T. Obsil
J Biol Chem 284, 19349-19360 (17 July 2009)

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
Proc. Natl. Acad. Sci. USA 105, 14680-14685 (23 September 2008)

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
J Biol Chem 283, 24899-24908 (5 September 2008)

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
J. Cell Sci. 119, 3613-3621 (1 September 2006)

Glucose Signaling in Saccharomyces cerevisiae
G. M. Santangelo, G. Link, M. Hoene, C. Russo, O. Selchow, and K. Pfizenmaier
Microbiol. Mol. Biol. Rev. 70, 253-282 (1 March 2006)

14-3-3{eta} is a novel regulator of parkin ubiquitin ligase
S. Sato, T. Chiba, E. Sakata, K. Kato, Y. Mizuno, N. Hattori, and K. Tanaka
EMBO J. 25, 211-221 (11 January 2006)

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
J. Immunol. 174, 7883-7893 (15 June 2005)

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
Bioinformatics 21, 2101-2103 (1 January 2005)

Science Signaling. ISSN 1937-9145 (online), 1945-0877 (print). Pre-2008: Science's STKE. ISSN 1525-8882