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We are analyzing https://www.nature.com/articles/353670a0.

Title:
Phosphorylation of c-jun mediated by MAP kinases | Nature
Description:
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 stimuli1โ€“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.
Website Age:
30 years and 10 months (reg. 1994-08-11).

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๐ŸŒ  Phenomenal Traffic: 5M - 10M visitors per month


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Keywords {๐Ÿ”}

article, nature, pubmed, google, scholar, cas, access, cjun, content, phosphorylation, cookies, kyriakis, avruch, ads, cell, privacy, map, open, research, data, cancer, advertising, information, journal, subscribe, october, kinases, pulverer, woodgett, transcription, response, regulates, activity, kinase, institution, buy, biol, tjian, services, permissions, function, optional, media, personal, parties, policy, journals, log, mediated, bernd,

Topics {โœ’๏ธ}

nature portfolio permissions reprints privacy policy medical services cancer research advertising social media subscribe nature repressing c-jun expression nature 332 nature 351 nature 343 nature 334 nature 352 nature 353 nature proto-oncogene c-jun personal data mitogen-activated protein-serine c-jun mediated data protection springerlink instant access permissions factor recruitment christopher phosphorylation positively regulates c-jun protein map kinase activation privacy explore content subscription content european economic area nuclear events elicited serine/threonine phosphorylation6 institutional subscriptions read intrinsic temporal order negative feedback mechanism mapk pathway inactivation eleni nikolakakiย &ย james hepatocellular carcinoma initiation accepting optional cookies journals search log issue learn harvard medical school article purchase manage preferences massachusetts general hospital journal publish coordinated antioxidant response transcription factor article cite

Schema {๐Ÿ—บ๏ธ}

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      headline:Phosphorylation of c-jun mediated by MAP kinases
      description: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 stimuli1รขย€ย“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.
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