Evidence map›Paper›PMID 16809764›Full record

ArticleMolecular and cellular biology2006

Histone deacetylase 8 safeguards the human ever-shorter telomeres 1B (hEST1B) protein from ubiquitin-mediated degradation.

Heehyoung Lee, Nilanjan Sengupta, Alejandro Villagra, Natalie Rezai-Zadeh, Edward Seto

Erratum issuedOpen access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
2.3field-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

44 citing papers in PubMed, 86 citations in OpenAlex.

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4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

5 authors at 1 institution in 1 country.

Heehyoung LeeH. Lee Moffitt Cancer Center & Research Institute, 12902 Magnolia Drive, Tampa, FL 33612, USA.
Nilanjan Sengupta
Alejandro Villagra
Natalie Rezai-Zadeh
Edward Seto
Moffitt Cancer Center · US

Funding

FUNCTIONAL ANALYSIS OF MAMMALIAN HISTONE DEACETYLASESR01GM058486 · NIGMS · UNIVERSITY OF SOUTH FLORIDA · PI SETO, EDWARD · 1999 to 2006
$2.3M
Regulation and Functions of Human Histone Deacetylase 8R01CA109699 · NCI · H. LEE MOFFITT CANCER CTR &RES INST · PI SETO, EDWARD · 2004 to 2008
$1.5M
NCI NIH HHS CA109699NCI NIH HHS R01 CA109699NIGMS NIH HHS GM58486NIGMS NIH HHS R01 GM058486
6 · The paper itself

Abstract

Histone deacetylases (HDACs) are enzymes that regulate the functions of histones as well as nonhistones by catalyzing the removal of acetyl groups from lysine residues. HDACs regulate many biological processes, including the cell division cycle and tumorigenesis. Although recent studies have implicated HDAC8 in tumor cell proliferation, the molecular mechanisms linking HDAC8 to cell growth remain unknown. Here, we report that the human ortholog of the yeast ever-shorter telomeres 1B (EST1B) binds HDAC8. This interaction is regulated by protein kinase A-mediated HDAC8 phosphorylation and protects human EST1B (hEST1B) from ubiquitin-mediated degradation. Phosphorylated HDAC8 preferentially recruits Hsp70 to a complex that inhibits the CHIP (C-terminal heat shock protein interacting protein) E3 ligase-mediated degradation of hEST1B. Importantly, HDAC8 regulation of hEST1B protein stability modulates total telomerase enzymatic activity. Our findings reveal a novel mechanism by which HDAC8 contributes to tumorigenesis by regulating telomerase activity.

Indexed as

AcetylationBase SequenceCyclic AMP-Dependent Protein KinasesDNA-Binding ProteinsDNA, ComplementaryGene SilencingHeLa CellsHistone DeacetylasesHSP70 Heat-Shock ProteinsHSP90 Heat-Shock ProteinsHumansIn Vitro TechniquesMultiprotein ComplexesPhosphorylationProtein BindingRecombinant ProteinsCyclic AMP-Dependent Protein KinasesDNA-Binding ProteinsDNA, ComplementaryHDAC8 protein, humanHistone DeacetylasesHSP70 Heat-Shock ProteinsHSP90 Heat-Shock ProteinsMultiprotein ComplexesRecombinant ProteinsRepressor ProteinsSTUB1 protein, humanTelomeraseUbiquitinUbiquitin-Protein Ligases

Identifiers

PMID16809764
PMCPMC1592721
OpenAlexW2101691020

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.