Evidence map›Paper›PMID 20691163›Full record

ArticleBiochemical and biophysical research communications2010

The Ski protein negatively regulates Siah2-mediated HDAC3 degradation.

Hong-Ling Zhao, Nobuhide Ueki, Michael J Hayman

Open access · greenAbstract read
In one paragraph

Article in Biochemical and biophysical research communications, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.1field-weighted citation impact, top 24% 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

21 citing papers in PubMed, 29 citations in OpenAlex.

  1. Article
  2. Review
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  6. Article
  7. Article
  8. Role of HDAC3-miRNA-CAGE Network in Anti-Cancer Drug-Resistance.International journal of molecular sciences · 2018
    Review
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  18. Article
  19. Regulators and effectors of Siah ubiquitin ligases.Cell biochemistry and biophysics · 2013
    Review
  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

3 authors at 1 institution in 1 country.

Hong-Ling ZhaoDepartment of Molecular Genetics and Microbiology, Stony Brook University, Stony Brook, NY 11794-5222, USA.
Nobuhide Ueki
Michael J Hayman
Stony Brook University · US

Funding

VIRAL ONCOLOGYT32CA009176 · NCI · STATE UNIVERSITY NEW YORK STONY BROOK · PI HEARING, PATRICK · 1985 to 2012
$5.2M
MECHANISM OF ACTION OF THE SKI ONCOGENER01CA042573 · NCI · STATE UNIVERSITY NEW YORK STONY BROOK · PI HAYMAN, MICHAEL JOHN · 1986 to 2005
$1.7M
NCI NIH HHS CA42573NCI NIH HHS R01 CA042573NCI NIH HHS T32-CA009176
6 · The paper itself

Abstract

Ski acts as a transcriptional co-repressor by multiple direct and indirect interactions with several distinct repression complexes. Ski represses retinoic acid (RA) signaling by interacting with, and stabilizing, key components of the co-repressor complex, namely, HDAC3. However, little is known as to how the Ski protein can stabilize HDAC3. In the present study, we identified the Siah2 protein as a potential E3 ubiquitin ligase that mediated proteasomal degradation of HDAC3. Reciprocal co-immunoprecipitation assays further revealed that Ski interacts with Siah2. Furthermore, co-expression of the Ski protein stabilized the level of Siah2 protein. Since Siah2 regulates its own level of expression by self-degradation, the stabilization of Siah2 by Ski is an indication that Ski association leads to inhibition of Siah2 E3 ubiquitin ligase activity. Only wild-type Ski and Ski truncation mutants that were in the same complex with Siah2 could stabilize HDAC3 levels. Taken together, the results suggest that association with Ski leads to inhibition of Siah2 E3 ubiquitin ligase activity and in this way, the Ski protein inhibits Siah2-mediated proteasomal degradation of HDAC3.

Indexed as

AnimalsChlorocebus aethiopsCOS CellsCysteine Proteinase InhibitorsDNA-Binding ProteinsEnzyme StabilityHistone Deacetylase 3Histone DeacetylasesHumansImmunoprecipitationLeupeptinsNuclear ProteinsProteasome Endopeptidase ComplexProteasome InhibitorsProto-Oncogene ProteinsSeven in Absentia Proteinsbenzyloxycarbonylleucyl-leucyl-leucine aldehydeCysteine Proteinase InhibitorsDNA-Binding ProteinsHistone Deacetylase 3Histone DeacetylasesLeupeptinsNuclear ProteinsProteasome Endopeptidase ComplexProteasome InhibitorsProto-Oncogene ProteinsSeven in Absentia ProteinsSKI protein, humanUbiquitin-Protein Ligases

Identifiers

PMID20691163
PMCPMC2940706
OpenAlexW2023782156

What OpenQuestion holds

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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.