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Structural basis for corepressor assembly by the orphan nuclear receptor TLX.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Zhi, Xiaoyong Zhou, X. Edward He, Yuanzheng Searose-Xu, Kelvin Zhang, Chun-Li Tsai, Chih-Cheng Melcher, Karsten Xu, H. Eric
Description	Author Affiliation: Zhi X ( Laboratory of Structural Sciences, Van Andel Research Institute, Grand Rapids, Michigan 49503, USA); Zhou XE ( Laboratory of Structural Sciences, Van Andel Research Institute, Grand Rapids, Michigan 49503, USA); He Y ( Laboratory of Structural Sciences, Van Andel Research Institute, Grand Rapids, Michigan 49503, USA); Searose-Xu K ( Laboratory of Structural Sciences, Van Andel Research Institute, Grand Rapids, Michigan 49503, USA); Zhang CL ( Department of Molecular Biology, University of Texas Southwestern Medical Center, Texas 75390, USA); Tsai CC ( Department of Cell Biology and Neuroscience, University of California at Riverside, Riverside, California 92521, USA); Melcher K ( Laboratory of Structural Sciences, Van Andel Research Institute, Grand Rapids, Michigan 49503, USA); Xu HE ( Laboratory of Structural Sciences, Van Andel Research Institute, Grand Rapids, Michigan 49503, USA)
Abstract	The orphan nuclear receptor TLX regulates neural stem cell self-renewal in the adult brain and functions primarily as a transcription repressor through recruitment of Atrophin corepressors, which bind to TLX via a conserved peptide motif termed the Atro box. Here we report crystal structures of the human and insect TLX ligand-binding domain in complex with Atro box peptides. In these structures, TLX adopts an autorepressed conformation in which its helix H12 occupies the coactivator-binding groove. Unexpectedly, H12 in this autorepressed conformation forms a novel binding pocket with residues from helix H3 that accommodates a short helix formed by the conserved ALXXLXXY motif of the Atro box. Mutations that weaken the TLX-Atrophin interaction compromise the repressive activity of TLX, demonstrating that this interaction is required for Atrophin to confer repressor activity to TLX. Moreover, the autorepressed conformation is conserved in the repressor class of orphan nuclear receptors, and mutations of corresponding residues in other members of this class of receptors diminish their repressor activities. Together, our results establish the functional conservation of the autorepressed conformation and define a key sequence motif in the Atro box that is essential for TLX-mediated repression.
File Format	HTM / HTML
ISSN	08909369
e-ISSN	15495477
DOI	10.1101/gad.254904.114
Journal	Genes & Development
Issue Number	4
Volume Number	29
Language	English
Publisher	Cold Spring Harbor Laboratory Press
Publisher Date	2015-02-15
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Discipline Molecular Discipline Biology__semicolon__developmental Discipline Biology__semicolon__genetics__semicolon__cell Discipline Biology Drosophila Melanogaster Chemistry Models, Molecular Orphan Nuclear Receptors Receptors, Cytoplasmic And Nuclear Animals Crystallization Drosophila Proteins Metabolism Hek293 Cells Research Support, N.i.h., Extramural
Content Type	Text
Resource Type	Article
Subject	Genetics Developmental Biology

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