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Cited by 195

The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.

c-Jun N-Terminal Phosphorylation Correlates with Activation of the JNK Subgroup but Not the ERK Subgroup of Mitogen-Activated Protein Kinases

Minden, A, Lin, A, Smeal, T, Dérijard, B, Cobb, M, Davis, R, Karin, M·1994·Molecular and Cellular Biology
DOI 10.1128/mcb.14.10.6683
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Abstract

c-Jun transcriptional activity is stimulated by phosphorylation at two N-terminal sites: Ser-63 and -73. Phosphorylation of these sites is enhanced in response to a variety of extracellular stimuli, including growth factors, cytokines, and UV irradiation. New members of the mitogen-activated protein (MAP) kinase group of signal-transducing enzymes, termed JNKs, bind to the activation domain of c-Jun and specifically phosphorylate these sites. However, the N-terminal sites of c-Jun were also suggested to be phosphorylated by two other MAP kinases, ERK1 and ERK2. Despite these reports, we find that unlike the JNKs, ERK1 and ERK2 do not phosphorylate the N-terminal sites of c-Jun in vitro; instead they phosphorylate an inhibitory C-terminal site. Furthermore, the phosphorylation of c-Jun in vivo at the N-terminal sites correlates with activation of the JNKs but not the ERKs. The ERKs are probably involved in the induction of c-fos expression and thereby contribute to the stimulation of AP-1 activity. Our study suggests that two different branches of the MAP kinase group are involved in the stimulation of AP-1 activity through two different mechanisms.

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Crossref · 10.1128/mcb.14.10.6683

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Metadata

Authors
Minden, A., Lin, A., Smeal, T., Dérijard, B., Cobb, M., Davis, R., & Karin, M.
Venue
Molecular and Cellular Biology
Publisher
Informa UK Limited
Published
1994-10
Volume
14
Issue
10
Pages
6683-6688
ISSN
  • 0270-7306
  • 1098-5549
DOI
10.1128/mcb.14.10.6683
Cited by
195
References
3
Language
en

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