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

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.

authors

Loriaux MM,Rehfuss RP,Brennan RG,Goodman RH

doi

10.1073/pnas.90.19.9046

subject

Has Abstract

pub_date

1993-10-01 00:00:00

pages

9046-50

issue

19

eissn

0027-8424

issn

1091-6490

journal_volume

90

pub_type

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