Evidence map›Paper›PMID 30910998›Full record

ArticleCell death & disease2019

BAG3 promotes autophagy and glutaminolysis via stabilizing glutaminase.

Song Zhao, Jia-Mei Wang, Jing Yan, Da-Lin Zhang, Bao-Qin Liu, Jing-Yi Jiang, Chao Li, Si Li, Xiao-Na Meng, Hua-Qin Wang

Open access · goldAbstract read
In one paragraph

Article in Cell death & disease, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed, 1 pooled it
3.4field-weighted citation impact, top 8% 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

45 citing papers in PubMed, 1 synthesis or guideline pooled it, 62 citations in OpenAlex.

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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

10 authors at 2 institutions in 2 countries.

Song ZhaoDepartment of Biochemistry & Molecular Biology, China Medical University, Shenyang, 110026, China.
Jia-Mei WangDepartment of Biochemistry & Molecular Biology, China Medical University, Shenyang, 110026, China.
Jing YanDepartment of Biochemistry & Molecular Biology, China Medical University, Shenyang, 110026, China.
Da-Lin ZhangDepartment of Thyroid Surgery, The 1st Affiliated Hospital, China Medical University, Shenyang, 110001, China.
Bao-Qin LiuDepartment of Biochemistry & Molecular Biology, China Medical University, Shenyang, 110026, China.
Jing-Yi JiangDepartment of Biochemistry & Molecular Biology, China Medical University, Shenyang, 110026, China.
Chao LiDepartment of Biochemistry & Molecular Biology, China Medical University, Shenyang, 110026, China.
Si LiDepartment of Biochemistry & Molecular Biology, China Medical University, Shenyang, 110026, China.
Xiao-Na MengDepartment of Biochemistry & Molecular Biology, China Medical University, Shenyang, 110026, China.
Hua-Qin WangDepartment of Biochemistry & Molecular Biology, China Medical University, Shenyang, 110026, China. hqwang@cmu.edu.cn.
China Medical University · CNJinzhou Medical University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Bcl-2 associated athanogene 3 (BAG3) is an important molecule that maintains oncogenic features of cancer cells via diverse mechanisms. One of the important functions assigned to BAG3 is implicated in selective macroautophagy/autophagy, which attracts much attention recently. However, the mechanism underlying regulation of autophagy by BAG3 has not been well defined. Here, we describe that BAG3 enhances autophagy via promotion of glutamine consumption and glutaminolysis. Glutaminolysis initiates with deamination of glutamine by glutaminase (GLS), by which yields glutamate and ammonia in mitochondria. The current study demonstrates that BAG3 stabilizes GLS via prohibition its interaction with SIRT5, thereby hindering its desuccinylation at Lys158 and Lys164 sites. As an underlying molecular mechanism, we demonstrate that BAG3 interacts with GLS and decreases SIRT5 expression. The current study also demonstrates that occupation by succinyl at Lys158 and Lys164 sites prohibits its Lys48-linked ubiquitination, thereby preventing its subsequent proteasomal degradation. Collectively, the current study demonstrates that BAG3 enhances autophagy via stabilizing GLS and promoting glutaminolysis. For the first time, this study reports that succinylation competes with ubiquitination to regulate proteasomal GLS degradation.

Indexed as

Adaptor Proteins, Signal TransducingAmmoniaApoptosis Regulatory ProteinsAutophagyEnzyme StabilityGlutaminaseGlutamineHep G2 CellsHumansMCF-7 CellsMitochondriaNeoplasmsProteasome Endopeptidase ComplexProteolysisSirtuinsTransfectionAdaptor Proteins, Signal TransducingAmmoniaApoptosis Regulatory ProteinsBAG3 protein, humanGlutaminaseGlutamineProteasome Endopeptidase ComplexSIRT5 protein, humanSirtuins

Identifiers

PMID30910998
PMCPMC6433946
OpenAlexW2925313069

What OpenQuestion holds

Textmetadata
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.