Requirement for integration of signals from two distinct phosphorylation pathways for activation of MAP kinase View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1990-02

AUTHORS

Neil G. Anderson, James L. Maller, Nicholas K. Tonks, Thomas W. Sturgill

ABSTRACT

MAP kinase (relative molecular mass, 42,000), a low abundance serine-threonine protein kinase, is transiently activated in many cell types by a variety of mitogens, including insulin, epidermal growth factor, and phorbol esters1,2. In vitro, MAP kinase will phosphorylate and reactivate S6 kinase II previously inactivated by phosphatase treatment3. Because many of the stimuli that activate MAP kinase are also stimulators of cell proliferation, and regulation of the cell cycle seems to involve a network of protein kinases, MAP kinase could be important in the transmission of stimuli eventually leading to the progression from GO to Gl in the cell cycle. Activated MAP kinase contains both phosphotyrosine and phosphothreonine4. We report here that MAP kinase can be deactivated completely by treatment with either phosphatase 2A, a protein phosphatase specific for phosphoserine and phosphothreonine, or CD45, a phosphotyrosine-specific protein phosphatase. We demonstrate that MAP kinase is only active when both tyrosyl and threonyl residues are phosphorylated and suggest therefore that the enzyme functions in vivo to integrate signals from two distinct transduction pathways. More... »

PAGES

651-653

Journal

TITLE

Nature

ISSUE

6259

VOLUME

343

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  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1038/343651a0

    DOI

    http://dx.doi.org/10.1038/343651a0

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1015375932

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/2154696


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