NDLI: Substrate recruitment to cyclin-dependent kinase 2 by a multipurpose docking site on cyclin A.

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Substrate recruitment to cyclin-dependent kinase 2 by a multipurpose docking site on cyclin A.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Harlow, E. Schulman, B. A. Lindstrom, D. L.
Description	Author Affiliation: Schulman BA ( Massachusetts General Hospital Cancer Center, Building 149, 13th Street, Charlestown, MA 02129, USA.);
Abstract	An important question in the cell cycle field is how cyclin-dependent kinases (cdks) target their substrates. We have studied the role of a conserved hydrophobic patch on the surface of cyclin A in substrate recognition by cyclin A-cdk2. This hydrophobic patch is approximately 35A away from the active site of cdk2 and contains the MRAIL sequence conserved among a number of mammalian cyclins. In the x-ray structure of cyclin A-cdk2-p27, this hydrophobic patch contacts the RNLFG sequence in p27 that is common to a number of substrates and inhibitors of mammalian cdks. We find that mutation of this hydrophobic patch on cyclin A eliminates binding to proteins containing RXL motifs without affecting binding to cdk2. This docking site is critical for cyclin A-cdk2 phosphorylation of substrates containing RXL motifs, but not for phosphorylation of histone H1. Impaired substrate binding by the cyclin is the cause of the defect in RXL substrate phosphorylation, because phosphorylation can be rescued by restoring a cyclin A-substrate interaction in a heterologous manner. In addition, the conserved hydrophobic patch is important for cyclin A function in cells, contributing to cyclin A's ability to drive cells out of the G1 phase of the cell cycle. Thus, we define a mechanism by which cyclins can recruit substrates to cdks, and our results support the notion that a high local concentration of substrate provided by a protein-protein interaction distant from the active site is critical for phosphorylation by cdks.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	18
Volume Number	95
Language	English
Publisher	National Academy of Sciences
Publisher Date	1998-09-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	CDC2-CDC28 Kinases Cyclin A Metabolism Cyclin-Dependent Kinases Protein-Serine-Threonine Kinases Amino Acid Sequence Cell Line Chemistry Cyclin-Dependent Kinase 2 Molecular Sequence Data Peptide Mapping Phosphorylation Protein Binding Substrate Specificity Research Support, U.S. Gov't, P.H.S. Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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