SMRT isoforms mediate repression and anti-repression of nuclear receptor heterodimers.
- 23 July 1996
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences of the United States of America
- Vol. 93 (15), 7567-7571
- https://doi.org/10.1073/pnas.93.15.7567
Abstract
Transcriptional repression represents an important component in the regulation of cell differentiation and oncogenesis mediated by nuclear hormone receptors. Hormones act to relieve repression, thus allowing receptors to function as transcriptional activators. The transcriptional corepressor SMRT was identified as a silencing mediator for retinoid and thyroid hormone receptors. SMRT is highly related to another corepressor, N-CoR, suggesting the existence of a new family of receptor-interacting proteins. We demonstrate that SMRT is a ubiquitous nuclear protein that interacts with unliganded receptor heterodimers in mammalian cells. Furthermore, expression of the receptor-interacting domain of SMRT acts as an antirepressor, suggesting the potential importance of splicing variants as modulators of thyroid hormone and retinoic acid signaling.Keywords
This publication has 37 references indexed in Scilit:
- The RXR heterodimers and orphan receptorsCell, 1995
- Functional inhibition of retinoic acid response by dominant negative retinoic acid receptor mutants.Proceedings of the National Academy of Sciences of the United States of America, 1993
- A mutated retinoic acid receptor-alpha exhibiting dominant-negative activity alters the lineage development of a multipotent hematopoietic cell line.Genes & Development, 1992
- A transferable silencing domain is present in the thyroid hormone receptor, in the v-erbA oncogene product and in the retinoic acid receptor.1992
- Ssn6-Tup1 is a general repressor of transcription in yeastCell, 1992
- The C'-terminal interaction domain of the thyroid hormone receptor confers the ability of the DNA site to dictate positive or negative transcriptional activity.Proceedings of the National Academy of Sciences of the United States of America, 1990
- Modular structure of a chicken lysozyme silencer: Involvement of an unusual thyroid hormone receptor binding siteCell, 1990
- Repression of transcription mediated at a thyroid hormone response element by the v-erb-A oncogene productNature, 1989
- Protein encoded by v-erbA functions as a thyroid-hormone receptor antagonistNature, 1989
- The c-erb-A protein is a high-affinity receptor for thyroid hormoneNature, 1986