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PMID: 1717989 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Mouse Erk-1 gene product is a serine/threonine protein kinase that has the potential to phosphorylate tyrosine.

Crews CM, Alessandrini AA, Erikson RL

Abstract

Bacterial expression of mouse gene Erk-1 yielded an active kinase with the same substrate specificity shown for ERK1 protein purified from rat cells. Although rat gene ERK1 is believed to encode a serine/threonine kinase based on sequence data and known ERK1 substrate phosphorylation sites, bacterially-produced mouse Erk-1 (bt-Erk-1) autophosphorylated on tyrosine in addition to serine and threonine residues. The bt-Erk-1 protein also had the capacity to reactivate the ribosomal protein S6 kinase (S6KII). Furthermore, treatment of bt-Erk-1 with either serine/threonine-specific phosphatase 2A or tyrosine-specific phosphatase 1B significantly decreased its kinase activity. These findings predict that autophosphorylation may play an important role in Erk-1/ERK1 regulation.

Related Genes
MeSH Terms
Amino Acid Sequence Animals Base Sequence Blotting, Western Calcium-Calmodulin-Dependent Protein Kinases Cloning, Molecular Mice Molecular Sequence Data Molecular Weight Myelin Basic Protein/metabolism Oligonucleotides/chemistry Phosphoprotein Phosphatases/metabolism Phosphoproteins/immunology,physiology Phosphotyrosine Polymerase Chain Reaction Protein Kinases/metabolism,physiology Protein Phosphatase 2 Protein Serine-Threonine Kinases Recombinant Proteins/metabolism Tyrosine/analogs & derivatives,metabolism
Chemicals
Myelin Basic Protein Oligonucleotides Phosphoproteins Recombinant Proteins Phosphotyrosine Tyrosine Protein Kinases Protein Serine-Threonine Kinases Calcium-Calmodulin-Dependent Protein Kinases Phosphoprotein Phosphatases Protein Phosphatase 2
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Crews C M
Department of Cellular and Developmental Biology, Harvard University, Cambridge, MA 02138.
Alessandrini A A
Erikson R L
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39 references, click to expand
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
Published
1991-10-01
Pages
8845-9
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC52607
Subset
IM
Grants
NCI NIH HHS · CA42580 · United States
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