Evidence map›Paper›PMID 26124119›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2015

Structural insights into the assembly of the histone deacetylase-associated Sin3L/Rpd3L corepressor complex.

Michael D Clark, Ryan Marcum, Richard Graveline, Clarence W Chan, Tao Xie, Zhonglei Chen, Yujia Ding, Yongbo Zhang, Alfonso Mondragón, Gregory David and 1 more

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
1.8field-weighted citation impact, top 15% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

38 citing papers in PubMed, 53 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. SDS3 regulates microglial inflammation by modulating the expression of the upstream kinase ASK1 in the p38 MAPK signaling pathway.Inflammation research : official journal of the European Histamine Research Society ... [et al.] · 2024
    Article
  6. The RPD3L deacetylation complex is required for facultative heterochromatin repression inProceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  7. Article
  8. Structure of histone deacetylase complex Rpd3S bound to nucleosome.Nature structural & molecular biology · 2023
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Structure of a SIN3-HDAC complex from budding yeast.Nature structural & molecular biology · 2023
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Article
  20. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

11 authors at 2 institutions in 1 country.

Michael D ClarkDepartment of Molecular Biosciences, Northwestern University, Evanston, IL 60208-3500;
Ryan MarcumDepartment of Molecular Biosciences, Northwestern University, Evanston, IL 60208-3500;
Richard GravelineDepartment of Pharmacology, New York University School of Medicine, New York City, NY 10016.
Clarence W ChanDepartment of Molecular Biosciences, Northwestern University, Evanston, IL 60208-3500;
Tao XieDepartment of Molecular Biosciences, Northwestern University, Evanston, IL 60208-3500;
Zhonglei ChenDepartment of Molecular Biosciences, Northwestern University, Evanston, IL 60208-3500;
Yujia DingDepartment of Molecular Biosciences, Northwestern University, Evanston, IL 60208-3500;
Yongbo ZhangDepartment of Molecular Biosciences, Northwestern University, Evanston, IL 60208-3500;
Alfonso MondragónDepartment of Molecular Biosciences, Northwestern University, Evanston, IL 60208-3500;
Gregory DavidDepartment of Pharmacology, New York University School of Medicine, New York City, NY 10016.
Ishwar RadhakrishnanDepartment of Molecular Biosciences, Northwestern University, Evanston, IL 60208-3500; i-radhakrishnan@northwestern.edu.
Northwestern University · USNew York University · US

Funding

Tumor Environment and Metastasis (TEAM) Research ProgramP30CA060553 · NCI · NORTHWESTERN UNIVERSITY AT CHICAGO · PI Daniela E Matei · 1993 to 2026
$153.9M
Vaccine FacilityP30CA016087 · NCI · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI ADRIANA HEGUY · 1985 to 2026
$83.1M
Molecular Biophysics Training Program at Northwestern UniversityT32GM008382 · NIGMS · NORTHWESTERN UNIVERSITY · PI RADHAKRISHNAN, ISHWAR · 1990 to 2020
$4.3M
Structural Biology of the Sin3 Corepressor ComplexR01GM064715 · NIGMS · NORTHWESTERN UNIVERSITY · PI RADHAKRISHNAN, ISHWAR · 2002 to 2011
$2.4M
600 MHz NMR Instrument Upgrade at Northwestern UniversityS10OD012016 · OD · NORTHWESTERN UNIVERSITY · PI RADHAKRISHNAN, ISHWAR · 2012 to 2012
$267k
NCI NIH HHS P30 CA016087NCI NIH HHS P30 CA060553NIGMS NIH HHS R01 GM064715NIGMS NIH HHS R01GM64715NIGMS NIH HHS T32 GM008382NIGMS NIH HHS T32GM008382NIH HHS S10 OD012016
6 · The paper itself

Abstract

Acetylation is correlated with chromatin decondensation and transcriptional activation, but its regulation by histone deacetylase (HDAC)-bearing corepressor complexes is poorly understood. Here, we describe the mechanism of assembly of the mammalian Sin3L/Rpd3L complex facilitated by Sds3, a conserved subunit deemed critical for proper assembly. Sds3 engages a globular, helical region of the HDAC interaction domain (HID) of the scaffolding protein Sin3A through a bipartite motif comprising a helix and an adjacent extended segment. Sds3 dimerizes through not only one of the predicted coiled-coil motifs but also, the segment preceding it, forming an ∼ 150-Å-long antiparallel dimer. Contrary to previous findings in yeast, Sin3A rather than Sds3 functions in recruiting HDAC1 into the complex by engaging the latter through a highly conserved segment adjacent to the helical HID subdomain. In the resulting model for the ternary complex, the two copies of the HDACs are situated distally and dynamically because of a natively unstructured linker connecting the dimerization domain and the Sin3A interaction domain of Sds3; these features contrast with the static organization described previously for the NuRD (nucleosome remodeling and deacetylase) complex. The Sds3 linker features several conserved basic residues that could potentially maintain the complex on chromatin by nonspecific interactions with DNA after initial recruitment by sequence-specific DNA-binding repressors.

Indexed as

Amino Acid SequenceAnimalsDimerizationHistone DeacetylasesMagnetic Resonance SpectroscopyMolecular Sequence DataProtein ConformationRepressor ProteinsSequence Homology, Amino AcidHistone DeacetylasesRepressor Proteinscorepressor complexhistone deacetylaseprotein–protein interactionstructural biologytranscription repression

Identifiers

PMID26124119
PMCPMC4507224
OpenAlexW1864559892

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.