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Molecular and Cellular Biology, December 2000, p. 9120-9126, Vol. 20, No. 24
0270-7306/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

DREAM-alpha CREM Interaction via Leucine-Charged Domains Derepresses Downstream Regulatory Element-Dependent Transcription

Fran Ledo, Angel M. Carrión, Wolfgang A. Link, Britt Mellström, and José R. Naranjo*

Departamento Biología Molecular y Celular, Centro Nacional de Biotecnología, CSIC, Madrid, Spain

Received 14 June 2000/Returned for modification 22 August 2000/Accepted 25 September 2000

Protein kinase A-dependent derepression of the human prodynorphin gene is regulated by the differential occupancy of the Dyn downstream regulatory element (DRE) site. Here, we show that a direct protein-protein interaction between DREAM and the CREM repressor isoform, alpha CREM, prevents binding of DREAM to the DRE and suggests a mechanism for cyclic AMP-dependent derepression of the prodynorphin gene in human neuroblastoma cells. Phosphorylation in the kinase-inducible domain of alpha CREM is not required for the interaction, but phospho-alpha CREM shows higher affinity for DREAM. The interaction with alpha CREM is independent of the Ca2+-binding properties of DREAM and is governed by leucine-charged residue-rich domains located in both alpha CREM and DREAM. Thus, our results propose a new mechanism for DREAM-mediated derepression that can operate independently of changes in nuclear Ca2+.

* Corresponding author. Mailing address: L115, CNB-CSIC, Campus Cantoblanco, 28049 Madrid, Spain. Phone: 34-91-5854682. Fax: 34-91-5854506. E-mail: naranjo{at}cnb.uam.es.

Molecular and Cellular Biology, December 2000, p. 9120-9126, Vol. 20, No. 24
0270-7306/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


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