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PMID: 11497994 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

The mechanism of protein kinase regulation by protein phosphatases.

Biochemical Society transactions ·Vol. 29 ·No. Pt 4 ·2001-08-00 ·Pages 385-91

Barford D

Abstract

Protein kinases are an important class of substrate of the protein phosphatases. We have examined the mechanism of dephosphorylation of the activation segments of the insulin receptor kinase and cyclin-dependent kinase 2 by their respective phosphatases, namely the tyrosine specific phosphatase PTP1B and the dual specificity phosphatase KAP. These studies reveal that PTP1B and KAP utilize contrasting mechanisms in order to dephosphorylate their substrates specifically.

MeSH Terms
Animals CDC2-CDC28 Kinases Cell Cycle Proteins Cyclin-Dependent Kinase 2 Cyclin-Dependent Kinase Inhibitor Proteins Cyclin-Dependent Kinases/metabolism Dual-Specificity Phosphatases Phosphoprotein Phosphatases/metabolism Protein Kinases/metabolism Protein Serine-Threonine Kinases/metabolism Protein Tyrosine Phosphatases Receptor, Insulin/metabolism Substrate Specificity
Chemicals
Cell Cycle Proteins Cyclin-Dependent Kinase Inhibitor Proteins Protein Kinases Receptor, Insulin Protein Serine-Threonine Kinases CDC2-CDC28 Kinases Cyclin-Dependent Kinase 2 Cyclin-Dependent Kinases Phosphoprotein Phosphatases CDKN3 protein, human Dual-Specificity Phosphatases Protein Tyrosine Phosphatases
Authors & Affiliations
1 authors, click to expand affiliations / ORCID
Barford D
Section of Structural Biology, Institute of Cancer Research, Chester Beatty Laboratories, 237 Fulham Road, London SW3 6JB, UK. dbarford@icr.ac.uk
Article Info
Journal
Biochemical Society transactions
Abbr.
Biochem Soc Trans
ISSN
0300-5127
Published
2001-08-00
Pages
385-91
Language
English
Region
England
NLM ID
7506897
Subset
IM
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