Engineered leucine zippers show that hemiphosphorylated CREB complexes are transcriptionally active.

Journal Article (Journal Article)

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.

Full Text

Duke Authors

Cited Authors

  • Loriaux, MM; Rehfuss, RP; Brennan, RG; Goodman, RH

Published Date

  • October 1, 1993

Published In

Volume / Issue

  • 90 / 19

Start / End Page

  • 9046 - 9050

PubMed ID

  • 8105470

Pubmed Central ID

  • PMC47498

International Standard Serial Number (ISSN)

  • 0027-8424

Digital Object Identifier (DOI)

  • 10.1073/pnas.90.19.9046


  • eng

Conference Location

  • United States