Evidence map›Paper›PMID 30209338›Full record

ArticleScientific reports2018

Differential HDAC1/2 network analysis reveals a role for prefoldin/CCT in HDAC1/2 complex assembly.

Charles A S Banks, Sayem Miah, Mark K Adams, Cassandra G Eubanks, Janet L Thornton, Laurence Florens, Michael P Washburn

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
2.0field-weighted citation impact, top 12% 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

29 citing papers in PubMed, 65 citations in OpenAlex.

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  16. Article
  17. Polycomb RequiresFrontiers in cell and developmental biology · 2021
    Article
  18. Prefoldin Function in Cellular Protein Homeostasis and Human Diseases.Frontiers in cell and developmental biology · 2021
    Review
  19. Article
  20. Article
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

7 authors at 1 institution in 1 country.

Charles A S BanksStowers Institute for Medical Research, Kansas City, MO, 64110, USA.
Sayem MiahStowers Institute for Medical Research, Kansas City, MO, 64110, USA.
Mark K AdamsStowers Institute for Medical Research, Kansas City, MO, 64110, USA.
Cassandra G EubanksStowers Institute for Medical Research, Kansas City, MO, 64110, USA.
Janet L ThorntonStowers Institute for Medical Research, Kansas City, MO, 64110, USA.
Laurence FlorensStowers Institute for Medical Research, Kansas City, MO, 64110, USA.
Michael P WashburnStowers Institute for Medical Research, Kansas City, MO, 64110, USA. mpw@stowers.org.ORCID 0000-0001-7568-2585
Stowers Institute for Medical Research · US

Funding

Inhibitor Reprogramming of a Human Histone Deacetylase Protein Interaction NetworkR01GM112639 · NIGMS · STOWERS INSTITUTE FOR MEDICAL RESEARCH · PI FLORENS, LAURENCE ALEXANDRA · 2016 to 2020
$1.6M
Characterization of the SIN3A and SIN3B HDAC complexesF32GM122215 · NIGMS · STOWERS INSTITUTE FOR MEDICAL RESEARCH · PI ADAMS, MARK K · 2017 to 2018
$116k
NIGMS NIH HHS F32 GM122215NIGMS NIH HHS R01 GM112639
6 · The paper itself

Abstract

HDAC1 and HDAC2 are components of several corepressor complexes (NuRD, Sin3, CoREST and MiDAC) that regulate transcription by deacetylating histones resulting in a more compact chromatin environment. This limits access of transcriptional machinery to genes and silences transcription. While using an AP-MS approach to map HDAC1/2 protein interaction networks, we noticed that N-terminally tagged versions of HDAC1 and HDAC2 did not assemble into HDAC corepressor complexes as expected, but instead appeared to be stalled with components of the prefoldin-CCT chaperonin pathway. These N-terminally tagged HDACs were also catalytically inactive. In contrast to the N-terminally tagged HDACs, C-terminally tagged HDAC1 and HDAC2 captured complete histone deacetylase complexes and the purified proteins had deacetylation activity that could be inhibited by SAHA (Vorinostat), a Class I/II HDAC inhibitor. This tag-mediated reprogramming of the HDAC1/2 protein interaction network suggests a mechanism whereby HDAC1 is first loaded into the CCT complex by prefoldin to complete folding, and then assembled into active, functional HDAC complexes. Imaging revealed that the prefoldin subunit VBP1 colocalises with nuclear HDAC1, suggesting that delivery of HDAC1 to the CCT complex happens in the nucleus.

Indexed as

Cell LineCell Line, TumorCell NucleusHEK293 CellsHeLa CellsHistone Deacetylase 1Histone Deacetylase 2Histone Deacetylase InhibitorsHumansMolecular ChaperonesProtein Interaction MapsRepressor ProteinsHDAC1 protein, humanHDAC2 protein, humanHistone Deacetylase 1Histone Deacetylase 2Histone Deacetylase InhibitorsMolecular ChaperonesprefoldinRepressor Proteins

Identifiers

PMID30209338
PMCPMC6135828
OpenAlexW2889931955

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.