Evidence map›Paper›PMID 26218645›Full record

ArticleAutophagy2015

SLC9A3R1 stimulates autophagy via BECN1 stabilization in breast cancer cells.

Hong Liu, Yan Ma, Hong-Wei He, Jia-Ping Wang, Jian-Dong Jiang, Rong-Guang Shao

Open access · bronzeAbstract read
In one paragraph

Article in Autophagy, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed, 2 pooled it
2.8field-weighted citation impact, top 9% 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

28 citing papers in PubMed, 2 syntheses or guidelines pooled it, 46 citations in OpenAlex.

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  16. Degradation Mechanism of Autophagy-Related Proteins and Research Progress.International journal of molecular sciences · 2022
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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

6 authors at 3 institutions in 1 country.

Hong Liua Department of Oncology ; Institute of Medicinal Biotechnology; Peking Union Medical College; Chinese Academy of Medical Sciences ; Beijing , China.
Yan Maa Department of Oncology ; Institute of Medicinal Biotechnology; Peking Union Medical College; Chinese Academy of Medical Sciences ; Beijing , China.
Hong-Wei Hea Department of Oncology ; Institute of Medicinal Biotechnology; Peking Union Medical College; Chinese Academy of Medical Sciences ; Beijing , China.
Jia-Ping Wangb China Astronaut Research and Training Center ; Beijing , China.
Jian-Dong Jianga Department of Oncology ; Institute of Medicinal Biotechnology; Peking Union Medical College; Chinese Academy of Medical Sciences ; Beijing , China.
Rong-Guang Shaoa Department of Oncology ; Institute of Medicinal Biotechnology; Peking Union Medical College; Chinese Academy of Medical Sciences ; Beijing , China.
Institute of Medicinal Plant Development · CNPeking Union Medical College Hospital · CNChina Astronaut Research and Training Center · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Autophagy, a self-catabolic process, has been found to be involved in abrogating the proliferation and metastasis of breast cancer. SLC9A3R1 (solute carrier family 9, subfamily A [NHE3, cation proton antiporter 3], member 3 regulator 1), a multifunctional scaffold protein, is involved in suppressing breast cancer cells proliferation and the SLC9A3R1-related signaling pathway regulates the activation of autophagy processes. However, the precise regulatory mechanism and signaling pathway of SLC9A3R1 in the regulation of autophagy processes in breast cancer cells remains unknown. Here, we report that the stability of BECN1, the major component of the autophagic core lipid kinase complex, is augmented in SLC9A3R1-overexpressing breast cancer MDA-MB-231 cells, subsequently stimulating autophagy by attenuating the interaction between BECN1 and BCL2. Initially, we found that SLC9A3R1 partially stimulated autophagy through the PTEN-PI3K-AKT1 signaling cascade in MDA-MB-231 cells. SLC9A3R1 then attenuated the interaction between BECN1 and BCL2 to stimulate the autophagic core lipid kinase complex. Further findings revealed that SLC9A3R1 bound to BECN1 and subsequently blocked ubiquitin-dependent BECN1 degradation. And the deletion of the C-terminal domain of SLC9A3R1 resulted in significantly reduced binding to BECN1. Moreover, the lack of C-terminal of SLC9A3R1 neither reduced the ubiquitination of BECN1 nor induced autophagy in breast cancer cells. The decrease in BECN1 degradation induced by SLC9A3R1 resulted in the activity of autophagy stimulation in breast cancer cells. These findings indicate that the SLC9A3R1-BECN1 signaling pathway participates in the activation of autophagy processes in breast cancer cells.

Indexed as

ApoptosisApoptosis Regulatory ProteinsAutophagyBeclin-1Breast NeoplasmsCell Line, TumorFemaleHumansMembrane ProteinsPhosphoproteinsSignal TransductionSodium-Hydrogen ExchangersUbiquitinUbiquitinationApoptosis Regulatory ProteinsBeclin-1BECN1 protein, humanMembrane ProteinsPhosphoproteinssodium-hydrogen exchanger regulatory factorSodium-Hydrogen ExchangersUbiquitinbreast cancer cellsprotein interactionprotein stabilitySLC9A3R1 signaling pathway, stimulating autophagyubiquitination degradation

Identifiers

PMID26218645
PMCPMC4835148
OpenAlexW1867296623

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.