Evidence map›Paper›PMID 25739441›Full record

ArticleThe Journal of biological chemistry2015

Endoplasmic reticulum (ER) localization is critical for DsbA-L protein to suppress ER stress and adiponectin down-regulation in adipocytes.

Meilian Liu, Hongzhi Chen, Li Wei, Derong Hu, Kun Dong, Weiping Jia, Lily Q Dong, Feng Liu

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
3.1field-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

25 citing papers in PubMed, 42 citations in OpenAlex.

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  20. Hepatic DsbA-L protects mice from diet-induced hepatosteatosis and insulin resistance.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2017
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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 4 institutions in 2 countries.

Meilian LiuFrom the Metabolic Syndrome Research Center, the Second Xiangya Hospital, Central South University, Changsha, Hunan 410011, China, the Departments of Biochemistry and Molecular Biology, University of New Mexico Health Science Center, Albuquerque, New Mexico 87131.
Hongzhi ChenFrom the Metabolic Syndrome Research Center, the Second Xiangya Hospital, Central South University, Changsha, Hunan 410011, China, Biochemistry, and.
Li Weithe Departments of Pharmacology, the Department of Endocrinology and Metabolism, Shanghai Diabetes Institute, Shanghai Key Laboratory of Diabetes Mellitus, Shanghai Clinical Center for Diabetes, Shanghai Jiao Tong University Affiliated Sixth People's Hospital, Shanghai 200025, China.
Derong Huthe Departments of Pharmacology.
Kun Dongthe Department of Endocrinology and Metabolism, Shanghai Diabetes Institute, Shanghai Key Laboratory of Diabetes Mellitus, Shanghai Clinical Center for Diabetes, Shanghai Jiao Tong University Affiliated Sixth People's Hospital, Shanghai 200025, China Cellular and Structural Biology, University of Texas Health Science Center at San Antonio (UTHSCSA), San Antonio, Texas 78229, and.
Weiping Jiathe Department of Endocrinology and Metabolism, Shanghai Diabetes Institute, Shanghai Key Laboratory of Diabetes Mellitus, Shanghai Clinical Center for Diabetes, Shanghai Jiao Tong University Affiliated Sixth People's Hospital, Shanghai 200025, China.
Lily Q DongCellular and Structural Biology, University of Texas Health Science Center at San Antonio (UTHSCSA), San Antonio, Texas 78229, and.
Feng LiuFrom the Metabolic Syndrome Research Center, the Second Xiangya Hospital, Central South University, Changsha, Hunan 410011, China, Biochemistry, and the Departments of Pharmacology, LiuF@uthscsa.edu.
The University of Texas Health Science Center at San Antonio · USCentral South University · CNShanghai Sixth People's Hospital · CNSecond Xiangya Hospital of Central South University · CN

Funding

Regulation and Function of Adiponectin OligomerizationR01DK076902 · NIDDK · UNIVERSITY OF TEXAS HLTH SCIENCE CENTER · PI LIU, FENG · 2008 to 2017
$2.9M
Mechanisms of cross talk between insulin and adiponectin signaling pathwaysR01DK080344 · NIDDK · UNIVERSITY OF TEXAS HLTH SCIENCE CENTER · PI DONG, LILY Q · 2009 to 2013
$1.8M
NIDDK NIH HHS R01 DK076902NIDDK NIH HHS R01 DK080344NIDDK NIH HHS R01 DK76902
6 · The paper itself

Abstract

Adiponectin is an adipokine with insulin-sensitizing and anti-inflammatory functions. We previously reported that adiponectin multimerization and stability are promoted by the disulfide bond A oxidoreductase-like protein (DsbA-L) in cells and in vivo. However, the precise mechanism by which DsbA-L regulates adiponectin biosynthesis remains elusive. Here we show that DsbA-L is co-localized with the endoplasmic reticulum (ER) marker protein disulfide isomerase and the mitochondrial marker MitoTracker. In addition, DsbA-L interacts with the ER chaperone protein Ero1-Lα in 3T3-L1 adipocytes. In silico analysis and truncation mapping studies revealed that DsbA-L contains an ER targeting signal at its N terminus. Deletion of the first 6 residues at the N terminus greatly impaired DsbA-L localization in the ER. Overexpression of the wild type but not the ER localization-defective mutant of DsbA-L protects against thapsigargin-induced ER stress and adiponectin down-regulation in 3T3-L1 adipocytes. In addition, overexpression of the wild type but not the ER localization-defective mutant of DsbA-L promotes adiponectin multimerization. Together, our results reveal that DsbA-L is localized in both the mitochondria and the ER in adipocytes and that its ER localization plays a critical role in suppressing ER stress and promoting adiponectin biosynthesis and secretion.

Indexed as

3T3-L1 CellsAdipocytesAdiponectinAnimalsCell DifferentiationEndoplasmic ReticulumEndoplasmic Reticulum StressGene Expression RegulationGlutathione TransferaseHEK293 CellsHumansMembrane GlycoproteinsMiceMitochondriaMutationOxidoreductasesAdiponectinADIPOQ protein, humanERO1A protein, humanGlutathione TransferaseGSTK1 protein, humanMembrane GlycoproteinsOxidoreductasesThapsigarginAdiponectinDsbA-LEndoplasmic Reticulum-associated Protein Degradation (ERAD)Endoplasmic Reticulum (ER)Endoplasmic Reticulum Stress (ER Stress)ER LocalizationMitochondria

Identifiers

PMID25739441
PMCPMC4400330
OpenAlexW2044802013

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.