Isolation of an AP-1 repressor by a novel method f...[Mol Cell Biol. 1997]

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1: Mol Cell Biol. 1997 Jun;17(6):3094-102. Links

Isolation of an AP-1 repressor by a novel method for detecting protein-protein interactions.

Aronheim A, Zandi E, Hennemann H, Elledge SJ, Karin M.

Department of Pharmacology, Program in Biomedical Sciences, School of Medicine, University of California, San Diego, La Jolla 92093-0636, USA.

Transcription factor AP-1 transduces environmental signals to the transcriptional machinery. To ensure a quick response yet maintain tight control over AP-1 target genes, AP-1 activity is likely to be negatively regulated in nonstimulated cells. To identify proteins that interact with the Jun subunits of AP-1 and repress its activity, we developed a novel screen for detecting protein-protein interactions that is not based on a transcriptional readout. In this system, the mammalian guanyl nucleotide exchange factor (GEF) Sos is recruited to the Saccharomyces cerevisiae plasma membrane harboring a temperature-sensitive Ras GEF, Cdc25-2, allowing growth at the nonpermissive temperature. Using the Sos recruitment system, we identified new c-Jun-interacting proteins. One of these, JDP2, heterodimerizes with c-Jun in nonstimulated cells and represses AP-1-mediated activation.

PMID: 9154808 [PubMed - indexed for MEDLINE]

PMCID: PMC232162

p75-Ras-GRF1 is a c-Jun/AP-1 target protein: its up regulation results in increased Ras activity and is necessary for c-Jun-induced nonadherent growth of Rat1a cells. [Mol Cell Biol. 2005]
B-ATF functions as a negative regulator of AP-1 mediated transcription and blocks cellular transformation by Ras and Fos. [Oncogene. 2000]
Long-range electrostatic interactions influence the orientation of Fos-Jun binding at AP-1 sites. [J Mol Biol. 2001]
Asymmetric recognition of nonconsensus AP-1 sites by Fos-Jun and Jun-Jun influences transcriptional cooperativity with NFAT1. [Mol Cell Biol. 2003]
ReviewAP-1 (Fos/Jun) transcription factors in hematopoietic differentiation and apoptosis. [Int J Oncol. 1998]

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Isolation of an AP-1 repressor by a novel method for detecting protein-protein interactions.

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