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PMID: 7644510 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

14-3-3 proteins associate with cdc25 phosphatases.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 92 ·No. 17 ·1995-08-15 ·Pages 7892-6

Conklin DS, Galaktionov K, Beach D

Abstract

The cdc25 phosphatases play key roles in cell cycle progression by activating cyclin-dependent kinases. Two members of the 14-3-3 protein family have been isolated in a yeast two-hybrid screen designed to identify proteins that interact with the human cdc25A and cdc25B phosphatases. Genes encoding the human homolog of the 14-3-3 epsilon protein and the previously described 14-3-3 beta protein have been isolated in this screening. 14-3-3 proteins constitute a family of well-conserved eukaryotic proteins that were originally isolated in mammalian brain preparations and that possess diverse biochemical activities related to signal transduction. We present evidence that indicates that cdc25 and 14-3-3 proteins physically interact both in vitro and in vivo. 14-3-3 protein does not, however, affect the phosphatase activity of cdc25A. Raf-1, which is known to bind 14-3-3 proteins, has recently been shown to associate with cdc25A and to stimulate its phosphatase activity. 14-3-3 protein, however, has no effect on the cdc25A-kinase activity of Raf-1. Instead, 14-3-3 may facilitate the association of cdc25 with Raf-1 in vivo, participating in the linkage between mitogenic signaling and the cell cycle machinery.

MeSH Terms
14-3-3 Proteins Amino Acid Sequence Animals Base Sequence Cell Cycle Proteins/isolation & purification,metabolism Cell Line Cloning, Molecular DNA, Complementary HeLa Cells Humans Molecular Sequence Data Phospholipases A/metabolism Phosphoprotein Phosphatases/isolation & purification,metabolism Protein Biosynthesis Protein Serine-Threonine Kinases/isolation & purification,metabolism Proteins/isolation & purification,metabolism Proto-Oncogene Proteins/isolation & purification,metabolism Proto-Oncogene Proteins c-raf Recombinant Fusion Proteins/biosynthesis,isolation & purification,metabolism Saccharomyces cerevisiae/metabolism Signal Transduction Spodoptera Transfection Tyrosine 3-Monooxygenase cdc25 Phosphatases
Chemicals
14-3-3 Proteins Cell Cycle Proteins DNA, Complementary Proteins Proto-Oncogene Proteins Recombinant Fusion Proteins Tyrosine 3-Monooxygenase Protein Serine-Threonine Kinases Proto-Oncogene Proteins c-raf Phospholipases A Phosphoprotein Phosphatases cdc25 Phosphatases
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Conklin D S
Howard Hughes Medical Institute, Cold Spring Harbor Laboratory, NY 11724, USA.
Galaktionov K
Beach D
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.92.17.7892
Published
1995-08-15
Pages
7892-6
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC41252
Subset
IM
Databases
GENBANK
U20972
External Links
PubMed source DOI: 10.1073/pnas.92.17.7892 PMC Full Text View journal details
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