NDLI: KAP: a dual specificity phosphatase that interacts with cyclin-dependent kinases.

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

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

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Hannon, G. J. Beach, D. Casso, D.
Description	Author Affiliation: Hannon GJ ( Howard Hughes Medical Institute, Cold Spring Harbor Laboratory, NY 11724.);
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.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	5
Volume Number	91
Language	English
Publisher	National Academy of Sciences
Publisher Date	1994-04-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	CDC2-CDC28 Kinases Cell Cycle Proteins Cyclin-Dependent Kinases Phosphoric Monoester Hydrolases Metabolism Protein Kinases Protein Tyrosine Phosphatases Protein-Serine-Threonine Kinases Amino Acid Sequence CDC2 Protein Kinase Cyclin-Dependent Kinase 2 Cyclin-Dependent Kinase Inhibitor Proteins DNA, Complementary Genetics Dual-Specificity Phosphatases Escherichia Coli G1 Phase Physiology HeLa Cells Molecular Sequence Data Phosphorylation Recombinant Fusion Proteins S Phase Substrate Specificity Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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