Engineered leucine zippers show that hemiphosphorylated CREB complexes are transcriptionally active

Marc M. Loriaux, Robert P. Rehfuss, Richard G. Brennan, Richard H. Goodman

Research output: Contribution to journalArticle

48 Scopus citations

Abstract

The ability of basic/leucine zipper transcription factors to form homo- and heterodimers potentially increases the diversity of signaling pathways that can impinge upon a single genetic element. The capacity of these proteins to dimerize in various combinations complicates the analysis of their functional properties, however. To simplify the functional analysis of CREB dimers, we mutated selected residues within the leucine zipper region to generate proteins that could only heterodimerize. These mutants allowed us to determine whether phosphorylation of both CREB subunits was necessary for transcriptional activation. Our results reveal that hemiphosphorylated CREB dimers are half as active as fully phosphorylated dimers. It is possible, therefore, that the degree of phosphorylation of CREB complexes could modulate the transcriptional responses of specific genes to cAMP.

Original languageEnglish (US)
Pages (from-to)9046-9050
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume90
Issue number19
DOIs
StatePublished - Oct 1 1993

Keywords

  • Cyclic AMP response element-binding protein
  • Protein kinase A
  • Transcription factor dimerization

ASJC Scopus subject areas

  • General

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