Galaktionov, K., Beach, D. (December 1991) Specific activation of cdc25 tyrosine phosphatases by B-type cyclins: evidence for multiple roles of mitotic cyclins. Cell, 67 (6). pp. 1181-94. ISSN 0092-8674 (Print)0092-8674 (Linking)
Abstract
Two previously unidentified human cdc25 genes have been isolated, cdc25A and cdc25B. Both genes rescue a cdc25ts mutant of fission yeast. Microinjection of anti-cdc25A antibodies into HeLa cells causes their arrest in mitosis. cdc25A and cdc25B display endogenous tyrosine phosphatase activity that is stimulated several-fold, in the absence of cdc2, by stoichiometric addition of either cyclin B1 or B2 but not A or D1. Association between cdc25A and cyclin B1/cdc2 was detected in the HeLa cells. These findings indicate that B-type cyclins are multifunctional proteins that not only act as M phase regulatory subunits of the cdc2 protein kinase, but also activate the cdc25 tyrosine phosphatase, of which cdc2 is the physiological substrate. A region of amino acid similarity between cyclins and tyrosine PTPases has been detected. This region is absent in cdc25 phosphatases. The motif may represent an activating domain that has to be provided to cdc25 by intermolecular interaction with cyclin B.
| Item Type: | Paper |
|---|---|
| Uncontrolled Keywords: | Amino Acid Sequence Base Sequence Cloning, Molecular Cyclins/*pharmacology DNA/genetics Enzyme Activation/drug effects Genetic Complementation Test HeLa Cells Humans Immunologic Techniques In Vitro Techniques *Mitosis Molecular Sequence Data Multigene Family Protein Tyrosine Phosphatases/*metabolism/*physiology Proteins/*physiology Schizosaccharomyces/genetics Sequence Alignment cdc25 Phosphatases |
| Subjects: | bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > Cyclins organs, tissues, organelles, cell types and functions > organelles, types and functions > mitosis bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > enzymes > protein tyrosine phosphatase |
| CSHL Authors: | |
| Communities: | CSHL labs > Beach lab |
| Depositing User: | Matt Covey |
| Date: | 20 December 1991 |
| Date Deposited: | 10 Dec 2015 20:49 |
| Last Modified: | 10 Dec 2015 20:49 |
| Related URLs: | |
| URI: | https://repository.cshl.edu/id/eprint/32149 |
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