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PMID: 2900470 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Phosphorylation-induced binding and transcriptional efficacy of nuclear factor CREB.

Nature ·Vol. 334 ·No. 6182 ·1988-08-11 ·Pages 494-8

Yamamoto KK, Gonzalez GA, Biggs WH, Montminy MR

Abstract

A nuclear protein, CREB, has been isolated from rat brain and shown to stimulate transcription of the cyclic AMP-responsive gene somatostatin as a dimer. Biochemical analysis suggests that dimerization and transcriptional efficacy of CREB protein in vitro are regulated by phosphorylation. These findings demonstrate that cellular signals can modulate gene expression by regulating the covalent modification of pre-existing nuclear factors.

MeSH Terms
Acetyltransferases/genetics Animals Brain Chemistry Chloramphenicol O-Acetyltransferase Chromatography Cyclic AMP/pharmacology DNA/metabolism Electrophoresis, Polyacrylamide Gel Macromolecular Substances Molecular Weight Nuclear Proteins/metabolism Phosphorylation Protein Kinase C/metabolism Protein Kinases/metabolism Rats Repetitive Sequences, Nucleic Acid Somatostatin/genetics Transcription, Genetic Transfection Tumor Cells, Cultured
Chemicals
Macromolecular Substances Nuclear Proteins Somatostatin DNA Cyclic AMP Acetyltransferases Chloramphenicol O-Acetyltransferase Protein Kinases Protein Kinase C
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Yamamoto K K
Clayton Foundation Laboratories for Peptide Biology, Salk Institute, La Jolla, California 92037.
Gonzalez G A
Biggs W H
Montminy M R
Article Info
Journal
Nature
Abbr.
Nature
ISSN
0028-0836
Published
1988-08-11
Pages
494-8
Language
English
Region
England
NLM ID
0410462
Subset
IM
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