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Cited by 219

The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.

Negative and positive regulation by transcription factor cAMP response element-binding protein is modulated by phosphorylation.

Open access
Lamph, W W, Dwarki, V J, Ofir, R, Montminy, M, Verma, I M·1990·Proceedings of the National Academy of Sciences

Abstract

We have shown that the transcriptional activity of the protooncogene jun (c-jun) promoter is repressed by a transcription factor, the cAMP response element-binding protein (CREB). This repression can be alleviated when CREB is phosphorylated by the catalytic subunit of protein kinase A. Repression cannot be alleviated by a mutant CREB deficient in the protein kinase A phosphorylation site (M1 CREB Ser-133----Ala), suggesting that phosphorylation of CREB at this site is essential for the relief of repression. Repression by CREB requires its binding to the c-jun promoter. In NIH 3T3 cells stably expressing CREB, c-jun is no longer induced by serum, but this repression can be relieved by treatment of the cells with forskolin, an agonist of the adenylate cyclase pathway. Thus, CREB has a dual function, that of a repressor in the absence of phosphorylation and an activator when phosphorylated by protein kinase A.

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Metadata

Authors
Lamph, W. W., Dwarki, V. J., Ofir, R., Montminy, M., & Verma, I. M.
Venue
Proceedings of the National Academy of Sciences
Published
1990-06
Volume
87
Issue
11
Pages
4320-4324
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
OpenAlex
W1980854045
Cited by
219
References
1
FWCI
9.32
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: Negative and positive regulation by transcription factor cAMP response element-binding protein is modulated by phosphorylation. https://app.cochat.ai/papers/10.1073/pnas.87.11.4320
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Lamph, W. W., Dwarki, V. J., Ofir, R., Montminy, M., & Verma, I. M. (1990). Negative and positive regulation by transcription factor cAMP response element-binding protein is modulated by phosphorylation. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.87.11.4320

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