Phosphorylation of c-jun mediated by MAP kinases View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1991-10

AUTHORS

Bernd J. Pulverer, John M. Kyriakis, Joseph Avruch, Eleni Nikolakaki, James R. Woodgett

ABSTRACT

THE proto-oncogene c-jun is a component of the AP-1 transcription factor family involved in the mediation of nuclear events elicited by extracellular stimuli1–3. The c-jun protein is negatively regulated by phosphorylation of residues near the carboxy terminus which are dephosphorylated in response to phorbol esters4. Here we identify two serine residues in the amino terminal Al transactivation domain which are phosphorylated in response to a variety of mitogens, phorbol esters and activated ras (ref. 5). We present evidence that mitogen-activated protein-serine (MAP) kinases (pp54 and pp42/44) specifically phosphorylate these sites and that their phosphorylation positively regulates the transacting activity of c-jun. The MAP kinase enzymes pp54 and pp42/44 are regulated by tyrosine as well as serine/threonine phosphorylation6,7. MAP kinase activation of c-jun may underlie the common stimulation of this transcription factor by mitogens, growth factors and oncogenes. More... »

PAGES

670-674

Journal

TITLE

Nature

ISSUE

6345

VOLUME

353

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/353670a0

DOI

http://dx.doi.org/10.1038/353670a0

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1030142073

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/1922387


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