Evidence map›Paper›PMID 33976119›Full record

ArticleCell death & disease2021

EGFR phosphorylates HDAC1 to regulate its expression and anti-apoptotic function.

Sonali Bahl, Hongbo Ling, Nuwan P N Acharige, Irene Santos-Barriopedro, Mary Kay H Pflum, Edward Seto

Open access · goldAbstract read
In one paragraph

Article in Cell death & disease, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

23 citing papers in PubMed, 30 citations in OpenAlex.

  1. Article
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  10. The deacetylases HDAC1/HDAC2 control JAK2Signal transduction and targeted therapy · 2025
    Article
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  18. Kinase-catalyzed crosslinking: A comparison of ATP-crosslinker analogs.Bioorganic & medicinal chemistry letters · 2024
    Article
  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

6 authors at 2 institutions in 1 country.

Sonali Bahl *Department of Biochemistry & Molecular Medicine, The George Washington University School of Medicine & Health Sciences, Washington, DC, USA.
Hongbo Ling *Department of Biochemistry & Molecular Medicine, The George Washington University School of Medicine & Health Sciences, Washington, DC, USA.
Nuwan P N AcharigeDepartment of Chemistry, Wayne State University, Detroit, MI, USA.
Irene Santos-BarriopedroDepartment of Biochemistry & Molecular Medicine, The George Washington University School of Medicine & Health Sciences, Washington, DC, USA.
Mary Kay H PflumDepartment of Chemistry, Wayne State University, Detroit, MI, USA.
Edward SetoDepartment of Biochemistry & Molecular Medicine, The George Washington University School of Medicine & Health Sciences, Washington, DC, USA. seto@gwu.edu.ORCID http://orcid.org/0000-0001-7562-7316
George Washington University · USWayne State University · US

Funding

Chemical Approaches to Study Protein Post-Translational ModificationsR35GM131821 · NIGMS · WAYNE STATE UNIVERSITY · PI Mary Kay H Pflum · 2019 to 2026
$4.3M
Supplement to Support Research Training in HDAC11 and CancerR01CA240529 · NCI · GEORGE WASHINGTON UNIVERSITY · PI LI, RONG, LIN, HENING · 2020 to 2024
$3.4M
Chemical Approaches to Mapping Cell Signaling PathwaysR01GM079529 · NIGMS · WAYNE STATE UNIVERSITY · PI PFLUM, MARY KAY H · 2009 to 2018
$2.5M
Targeting SIRT1 in Mantle Cell LymphomaR01CA187040 · NCI · H. LEE MOFFITT CANCER CTR & RES INST · PI SETO, EDWARD · 2014 to 2018
$1.6M
NCI NIH HHS R01 CA187040NCI NIH HHS R01 CA240529NIGMS NIH HHS R01 GM079529NIGMS NIH HHS R35 GM131821
6 · The paper itself

Abstract

HDAC1 is the prototypical human histone deacetylase (HDAC) enzyme responsible for catalyzing the removal of acetyl group from lysine residues on many substrate proteins. By deacetylating histones and non-histone proteins, HDAC1 has a profound effect on the regulation of gene transcription and many processes related to cell growth and cell death, including cell cycle progression, DNA repair, and apoptosis. Early studies reveal that, like most eukaryotic proteins, the functions and activities of HDAC1 are regulated by post-translational modifications. For example, serine phosphorylation of HDAC1 by protein kinase CK2 promotes HDAC1 deacetylase enzymatic activity and alters its interactions with proteins in corepressor complexes. Here, we describe an alternative signaling pathway by which HDAC1 activities are regulated. Specifically, we discover that EGFR activity promotes the tyrosine phosphorylation of HDAC1, which is necessary for its protein stability. A key EGFR phosphorylation site on HDAC1, Tyr72, mediates HDAC1's anti-apoptotic function. Given that HDAC1 overexpression and EGFR activity are strongly related with tumor progression and cancer cell survival, HDAC1 tyrosine phosphorylation may present a possible target to manipulate HDAC1 protein levels in future potential cancer treatment strategies.

Indexed as

ApoptosisErbB ReceptorsHistone Deacetylase 1HumansPhosphorylationTransfectionEGFR protein, humanErbB ReceptorsHDAC1 protein, humanHistone Deacetylase 1

Identifiers

PMID33976119
PMCPMC8113371
OpenAlexW3163140492

What OpenQuestion holds

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LicenceCC BY
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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.