KAP: A dual specificity phosphatase that interacts with cyclin-dependent kinases

Hannon, G. J., Casso, D., Beach, D. (1994) KAP: A dual specificity phosphatase that interacts with cyclin-dependent kinases. Proceedings of the National Academy of Sciences of the United States of America, 91 (5). pp. 1731-1735. ISSN 00278424 (ISSN)

URL: http://www.ncbi.nlm.nih.gov/pubmed/8127873
DOI: 10.1073/pnas.91.5.1731

Abstract

The cyclin-dependent kinases are key cell cycle regulators whose activation is required for passage from one cell cycle phase to the next. In mammalian cells, CDK2 has been implicated in control of the G1 and S phases. We have used a two-hybrid protein interaction screen to identify cDNAs encoding proteins that can interact with CDK2. Among those identified was a protein (KAP), which contained the HCXX-XXGR motif characteristic of protein tyrosine phosphatases. KAP showed phosphatase activity toward substrates containing either phosphotyrosine or phosphoserine residues. Since KAP is not significantly similar to known phosphatases beyond the catalytic core motif, it represents an additional class of dual specificity phosphatase. KAP interacted with cdc2 and CDK2 in yeast. In mammalian cells, KAP also associated with cdc2 and CDK2 but showed a preference for cdc2. The ability of KAP to bind multiple cyclin-dependent kinases suggests that it may play a role in cell cycle regulation.

Item Type: Paper
Uncontrolled Keywords: cdc2 CDK2 cell cycle binding protein cycline glutathione transferase hybrid protein iodoacetic acid mutant protein n ethylmaleimide okadaic acid phosphoserine phosphotransferase phosphotyrosine protein tyrosine phosphatase tartaric acid tetramisole vanadate sodium amino acid sequence animal cell article controlled study dephosphorylation enzyme activity enzyme specificity human human cell mammal cell nonhuman priority journal protein protein interaction Base Sequence DNA, Complementary Escherichia coli G1 Phase Hela Cells Molecular Sequence Data Phosphoric Monoester Hydrolases Phosphorylation Protein Kinases Protein p34cdc2 Protein-Tyrosine-Phosphatase Recombinant Fusion Proteins S Phase Substrate Specificity Support, Non-U.S. Gov't Support, U.S. Gov't, P.H.S. Animalia Mammalia
Subjects: bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > enzymes
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > enzymes > kinase
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > enzymes > protein phosphatase
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types
CSHL Authors:
Communities: CSHL labs > Hannon lab
Depositing User: Matt Covey
Date: 1994
Date Deposited: 09 Jan 2013 17:38
Last Modified: 09 Jan 2013 17:38
PMCID: PMC43237
Related URLs:
URI: http://repository.cshl.edu/id/eprint/26490

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