Evidence map›Paper›PMID 24820421›Full record

ArticleMolecular and cellular biology2014

Differential properties of transcriptional complexes formed by the CoREST family.

Álvaro P Barrios, Andrea V Gómez, Julián E Sáez, Giuseppe Ciossani, Emanuela Toffolo, Elena Battaglioli, Andrea Mattevi, María E Andrés

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Article in Molecular and cellular biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

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46citing papers in PubMed
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1 · What the graph read from it

What it found

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2 · The registry

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3 · Its place in the literature

Who cites it

46 citing papers in PubMed.

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4 · The record

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5 · Who and what money

Authors and funding

8 authors.

Álvaro P Barrios
Andrea V Gómez
Julián E Sáez
Giuseppe Ciossani
Emanuela Toffolo
Elena Battaglioli
Andrea Mattevi
María E Andrés

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Mammalian genomes harbor three CoREST genes. rcor1 encodes CoREST (CoREST1), and the paralogues rcor2 and rcor3 encode CoREST2 and CoREST3, respectively. Here, we describe specific properties of transcriptional complexes formed by CoREST proteins with the histone demethylase LSD1/KDM1A and histone deacetylases 1 and 2 (HDAC1/2) and the finding that all three CoRESTs are expressed in the adult rat brain. CoRESTs interact equally strongly with LSD1/KDM1A. Structural analysis shows that the overall conformation of CoREST3 is similar to that of CoREST1 complexed with LSD1/KDM1A. Nonetheless, transcriptional repressive capacity of CoREST3 is lower than that of CoREST1, which correlates with the observation that CoREST3 leads to a reduced LSD1/KDM1A catalytic efficiency. Also, CoREST2 shows a lower transcriptional repression than CoREST1, which is resistant to HDAC inhibitors. CoREST2 displays lower interaction with HDAC1/2, which is barely present in LSD1/KDM1A-CoREST2 complexes. A nonconserved leucine in the first SANT domain of CoREST2 severely weakens its association with HDAC1/2. Furthermore, CoREST2 mutants with increased HDAC1/2 interaction and those without HDAC1/2 interaction exhibit equivalent transcriptional repression capacities, indicating that CoREST2 represses in an HDAC-independent manner. In conclusion, differences among CoREST proteins are instrumental in the modulation of protein-protein interactions and catalytic activities of LSD1/KDM1A-CoREST-HDAC complexes, fine-tuning gene expression regulation.

Indexed as

AnimalsBrainCatalytic DomainCo-Repressor ProteinsGene Expression RegulationHEK293 CellsHistone DeacetylasesHistone DemethylasesHumansMaleModels, MolecularNerve Tissue ProteinsProtein ConformationRatsRats, Sprague-DawleyCo-Repressor ProteinsCoREST protein, ratHistone DeacetylasesHistone DemethylasesNerve Tissue ProteinsRCOR1 protein, human

Identifiers

PMID24820421
PMCPMC4097654

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.