Publication Date:
1998-06-20
Description:
MAP kinase phosphatase-3 (MKP-3) dephosphorylates phosphotyrosine and phosphothreonine and inactivates selectively ERK family mitogen-activated protein (MAP) kinases. MKP-3 was activated by direct binding to purified ERK2. Activation was independent of protein kinase activity and required binding of ERK2 to the noncatalytic amino-terminus of MKP-3. Neither the gain-of-function Sevenmaker ERK2 mutant D319N nor c-Jun amino-terminal kinase-stress-activated protein kinase (JNK/SAPK) or p38 MAP kinases bound MKP-3 or caused its catalytic activation. These kinases were also resistant to enzymatic inactivation by MKP-3. Another homologous but nonselective phosphatase, MKP-4, bound and was activated by ERK2, JNK/SAPK, and p38 MAP kinases. Catalytic activation of MAP kinase phosphatases through substrate binding may regulate MAP kinase activation by a large number of receptor systems.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Camps, M -- Nichols, A -- Gillieron, C -- Antonsson, B -- Muda, M -- Chabert, C -- Boschert, U -- Arkinstall, S -- New York, N.Y. -- Science. 1998 May 22;280(5367):1262-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Geneva Biomedical Research Institute, Glaxo Wellcome Research and Development S.A., CH-1228 Plan-les-Ouates, Geneva, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9596579" target="_blank"〉PubMed〈/a〉
Keywords:
Amino Acid Sequence
;
Animals
;
COS Cells
;
Calcium-Calmodulin-Dependent Protein Kinases/antagonists &
;
inhibitors/genetics/*metabolism
;
Catalysis
;
Dual Specificity Phosphatase 6
;
Enzyme Activation
;
Epidermal Growth Factor/pharmacology
;
Mitogen-Activated Protein Kinase 1
;
Mitogen-Activated Protein Kinase 12
;
Mitogen-Activated Protein Kinase 9
;
*Mitogen-Activated Protein Kinases
;
Molecular Sequence Data
;
Mutation
;
Phosphorylation
;
Protein Kinases/metabolism
;
Protein Tyrosine Phosphatases/genetics/*metabolism
;
Recombinant Fusion Proteins/metabolism
;
Signal Transduction
;
Transfection
;
p38 Mitogen-Activated Protein Kinases
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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