Evidence map›Paper›PMID 35387978›Full record

ArticleCell death & disease2022

HspBP1 is a dual function regulatory protein that controls both DNA repair and apoptosis in breast cancer cells.

Cha Kyung Youn, Jung-Hee Lee, Gurusamy Hariharasudhan, Hong Beum Kim, Jeeho Kim, Sumi Lee, Sung-Chul Lim, Sang-Pil Yoon, Sang-Gon Park, In-Youb Chang and 1 more

Open access · goldAbstract read
In one paragraph

Article in Cell death & disease, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.2field-weighted citation impact, top 22% 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

13 citing papers in PubMed, 15 citations in OpenAlex.

  1. Article
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  4. A Functional Study of the ApoptosisInternational journal of molecular sciences · 2026
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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

11 authors at 3 institutions in 1 country.

Cha Kyung Youn *DNA Damage Response Network Center, Chosun University School of Medicine, 375 Seosuk-dong, Gwangju, Republic of Korea.
Jung-Hee Lee *DNA Damage Response Network Center, Chosun University School of Medicine, 375 Seosuk-dong, Gwangju, Republic of Korea.
Gurusamy HariharasudhanDNA Damage Response Network Center, Chosun University School of Medicine, 375 Seosuk-dong, Gwangju, Republic of Korea.ORCID 0000-0001-5436-5740
Hong Beum KimDNA Damage Response Network Center, Chosun University School of Medicine, 375 Seosuk-dong, Gwangju, Republic of Korea.
Jeeho KimDNA Damage Response Network Center, Chosun University School of Medicine, 375 Seosuk-dong, Gwangju, Republic of Korea.
Sumi LeeDNA Damage Response Network Center, Chosun University School of Medicine, 375 Seosuk-dong, Gwangju, Republic of Korea.
Sung-Chul LimDNA Damage Response Network Center, Chosun University School of Medicine, 375 Seosuk-dong, Gwangju, Republic of Korea.
Sang-Pil YoonDepartment of Anatomy, School of Medicine, Jeju National University, Jeju-Do, Republic of Korea.
Sang-Gon ParkDepartment of Hemato-oncology, Chosun University Hospital Internal Medicine, Gwangju, Republic of Korea. sgpark@chosun.ac.kr.
In-Youb ChangDepartment of Anatomy, Chosun University School of Medicine, 375 Seosuk-dong, Gwangju, Republic of Korea. iyjang@chosun.ac.kr.ORCID 0000-0002-8911-7541
Ho Jin YouDNA Damage Response Network Center, Chosun University School of Medicine, 375 Seosuk-dong, Gwangju, Republic of Korea. hjyou@chosun.ac.kr.ORCID 0000-0002-0530-4017
Chosun University · KRChosun University Hospital · KRJeju National University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The Hsp70-binding protein 1 (HspBP1) belongs to a family of co-chaperones that regulate Hsp70 activity and whose biological significance is not well understood. In the present study, we show that when HspBP1 is either knocked down or overexpressed in BRCA1-proficient breast cancer cells, there were profound changes in tumorigenesis, including anchorage-independent cell growth in vitro and in tumor formation in xenograft models. However, HspBP1 did not affect tumorigenic properties in BRCA1-deficient breast cancer cells. The mechanisms underlying HspBP1-induced tumor suppression were found to include interactions with BRCA1 and promotion of BRCA1-mediated homologous recombination DNA repair, suggesting that HspBP1 contributes to the suppression of breast cancer by regulating BRCA1 function and thereby maintaining genomic stability. Interestingly, independent of BRCA1 status, HspBP1 facilitates cell survival in response to ionizing radiation (IR) by interfering with the association of Hsp70 and apoptotic protease-activating factor-1. These findings suggest that decreased HspBP1 expression, a common occurrence in high-grade and metastatic breast cancers, leads to genomic instability and enables resistance to IR treatment.

Indexed as

Breast NeoplasmsAdaptor Proteins, Signal TransducingApoptosisBRCA1 ProteinDNA RepairFemaleHSP70 Heat-Shock ProteinsHumansRecombinational DNA RepairAdaptor Proteins, Signal TransducingBRCA1 ProteinHSP70 Heat-Shock ProteinsHSPBP1 protein, human

Identifiers

PMID35387978
PMCPMC8986865
OpenAlexW4223411223

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LicenceCC BY
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Registered trials

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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.