Evidence map›Paper›PMID 34530730›Full record

ReviewMolecular medicine (Cambridge, Mass.)2021

Posttranslational modification and beyond: interplay between histone deacetylase 6 and heat-shock protein 90.

Ping Liu, Ji Xiao, Yiliang Wang, Xiaowei Song, Lianzhou Huang, Zhe Ren, Kaio Kitazato, Yifei Wang

Open access · goldAbstract readReview
In one paragraph

Review in Molecular medicine (Cambridge, Mass.), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed
4.7field-weighted citation impact, top 4% 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

53 citing papers in PubMed, 69 citations in OpenAlex.

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  14. [EJNMMI radiopharmacy and chemistry · 2025
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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

8 authors at 2 institutions in 2 countries.

Ping Liu *College of Life Science and Technology, Guangzhou Jinan Biomedicine Research and Development Center, Jinan University, Guangzhou, China.
Ji Xiao *College of Life Science and Technology, Guangzhou Jinan Biomedicine Research and Development Center, Jinan University, Guangzhou, China.
Yiliang WangCollege of Life Science and Technology, Guangzhou Jinan Biomedicine Research and Development Center, Jinan University, Guangzhou, China.
Xiaowei SongCollege of Life Science and Technology, Guangzhou Jinan Biomedicine Research and Development Center, Jinan University, Guangzhou, China.
Lianzhou HuangCollege of Life Science and Technology, Guangzhou Jinan Biomedicine Research and Development Center, Jinan University, Guangzhou, China.
Zhe RenCollege of Life Science and Technology, Guangzhou Jinan Biomedicine Research and Development Center, Jinan University, Guangzhou, China.
Kaio KitazatoDepartment of Clinical Research Pharmacy, Graduate School of Biomedical Sciences, Nagasaki University, Nagasaki, Japan. kitazato8@gmail.com.
Yifei WangCollege of Life Science and Technology, Guangzhou Jinan Biomedicine Research and Development Center, Jinan University, Guangzhou, China. twang-yf@163.com.ORCID 0000-0002-9918-2865
Jinan University · CNUniversity of Nagasaki · JP

Funding

national natural science foundation of china 82072274natural science foundation of guangdong province 2019A1515010046
6 · The paper itself

Abstract

Posttranslational modification (PTM) and regulation of protein stability are crucial to various biological processes. Histone deacetylase 6 (HDAC6), a unique histone deacetylase with two functional catalytic domains (DD1 and DD2) and a ZnF-UBP domain (ubiquitin binding domain, BUZ), regulates a number of biological processes, including gene expression, cell motility, immune response, and the degradation of misfolded proteins. In addition to the deacetylation of histones, other nonhistone proteins have been identified as substrates for HDAC6. Hsp90, a molecular chaperone that is a critical modulator of cell signaling, is one of the lysine deacetylase substrates of HDAC6. Intriguingly, as one of the best-characterized regulators of Hsp90 acetylation, HDAC6 is the client protein of Hsp90. In addition to regulating Hsp90 at the post-translational modification level, HDAC6 also regulates Hsp90 at the gene transcription level. HDAC6 mainly regulates the Hsp90-HSF1 complex through the ZnF-UBP domain, thereby promoting the HSF1 entry into the nucleus and activating gene transcription. The mutual interaction between HDAC6 and Hsp90 plays an important role in the regulation of protein stability, cell migration, apoptosis and other functions. Plenty of of studies have indicated that blocking HDAC6/Hsp90 has a vital regulatory role in multifarious diseases, mainly in cancers. Therefore, developing inhibitors or drugs against HDAC6/Hsp90 becomes a promising development direction. Herein, we review the current knowledge on molecular regulatory mechanisms based on the interaction of HDAC6 and Hsp90 and inhibition of HDAC6 and/or Hsp90 in oncogenesis and progression, antiviral and immune-related diseases and other vital biological processes.

Indexed as

Protein Processing, Post-TranslationalAcetylationAnimalsDrug DevelopmentDrug DiscoveryGene Expression RegulationHistone Deacetylase 6HistonesHSP90 Heat-Shock ProteinsHumansIsoenzymesProtein BindingSignal TransductionStructure-Activity RelationshipHistone Deacetylase 6HistonesHSP90 Heat-Shock ProteinsIsoenzymesAcetylationClient proteinsDrug developmentHDAC6Hsp90

Identifiers

PMID34530730
PMCPMC8444394
OpenAlexW3200164063

What OpenQuestion holds

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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.