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Cited by 2,134

The DOI matches its Crossref record; 14 of the 14 references it cites were found in a registry or an index.

CREB: A Stimulus-Induced Transcription Factor Activated by A Diverse Array of Extracellular Signals

Shaywitz, Adam J., Greenberg, Michael E.·1999·Annual Review of Biochemistry

Abstract

▪ Abstract Extracellular stimuli elicit changes in gene expression in target cells by activating intracellular protein kinase cascades that phosphorylate transcription factors within the nucleus. One of the best characterized stimulus-induced transcription factors, cyclic AMP response element (CRE) -binding protein (CREB), activates transcription of target genes in response to a diverse array of stimuli, including peptide hormones, growth factors, and neuronal activity, that activate a variety of protein kinases including protein kinase A (PKA), pp90 ribosomal S6 kinase (pp90RSK), and Ca2+/calmodulin-dependent protein kinases (CaMKs). These kinases all phosphorylate CREB at a particular residue, serine 133 (Ser133), and phosphorylation of Ser133 is required for CREB-mediated transcription. Despite this common feature, the mechanism by which CREB activates transcription varies depending on the stimulus. In some cases, signaling pathways target additional sites on CREB or proteins associated with CREB, permitting CREB to regulate distinct programs of gene expression under different conditions of stimulation. This review will discuss the molecular mechanisms by which Ser133--phosphorylated CREB activates transcription, intracellular signaling pathways that lead to phosphorylation of CREB at Ser133, and features of each signaling pathway that impart specificity at the level of CREB activation.

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Crossref · 10.1146/annurev.biochem.68.1.821

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Metadata

Authors
Shaywitz, A. J., & Greenberg, M. E.
Venue
Annual Review of Biochemistry
Published
1999-06
Volume
68
Issue
1
Pages
821-861
ISSN
  • 0066-4154 (ISSN-L)
  • 1545-4509
OpenAlex
W2137385309
Cited by
2,134
References
14
FWCI
5.10
Type
journal article
Language
en
Open access
closed

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