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PMID: 1322292 Published · ppublish English Comparative Study Journal Article Research Support, Non-U.S. Gov't

Xenopus MAP kinase activator is a serine/threonine/tyrosine kinase activated by threonine phosphorylation.

The EMBO journal ·Vol. 11 ·No. 8 ·1992-08-00 ·Pages 2903-8

Kosako H, Gotoh Y, Matsuda S, Ishikawa M, Nishida E

Abstract

Xenopus MAP kinase activator, a 45 kDa protein, has been shown to function as a direct upstream factor sufficient for full activation and both tyrosine and serine/threonine phosphorylation of inactive MAP kinase. We have now shown by using an anti-MAP kinase activator antiserum that MAP kinase activator is ubiquitous in tissues and is regulated post-translationally. Activation of MAP kinase activator is correlated precisely with its threonine phosphorylation during the oocyte maturation process. It is a key question whether MAP kinase activator is a kinase or not. We have shown that Xenopus MAP kinase activator purified from mature oocytes is capable of undergoing autophosphorylation on serine, threonine and tyrosine residues. Dephosphorylation of purified activator by protein phosphatase 2A treatment inactivates its autophosphorylation activity as well as its activator activity. Thus, Xenopus MAP kinase activator is a protein kinase with specificity for both serine/threonine and tyrosine. Partial protein sequencing of purified activator indicates that it contains a sequence homologous to kinase subdomains VI and VII of two yeast protein kinases, STE7 and byrl.

MeSH Terms
Amino Acid Sequence Animals Calcium-Calmodulin-Dependent Protein Kinases Immune Sera Immunoassay Kinetics Mitogen-Activated Protein Kinase Kinases Molecular Sequence Data Oocytes/enzymology,physiology Peptides/chemical synthesis,immunology Phosphorylation Protein Kinases/isolation & purification,metabolism Sequence Homology, Nucleic Acid Threonine Xenopus
Chemicals
Immune Sera Peptides Threonine Protein Kinases Calcium-Calmodulin-Dependent Protein Kinases Mitogen-Activated Protein Kinase Kinases
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Kosako H
Department of Biophysics and Biochemistry, Faculty of Science, University of Tokyo, Japan.
Gotoh Y
Matsuda S
Ishikawa M
Nishida E
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Article Info
Journal
The EMBO journal
Abbr.
EMBO J
ISSN
0261-4189
Published
1992-08-00
Pages
2903-8
Language
English
Region
England
NLM ID
8208664
PMCID
PMC556771
Subset
IM
External Links
PubMed source PMC Full Text View journal details
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