Evidence map›Paper›PMID 39909774›Full record

ReviewTrends in cell biology2025

Endoplasmic reticulum (ER) protein degradation by ER-associated degradation and ER-phagy.

Shuangcheng Alivia Wu, Zexin Jason Li, Ling Qi

Abstract readReview
In one paragraph

Review in Trends in cell biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
–field-weighted citation impact
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

26 citing papers in PubMed.

  1. Review
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  6. SEL1L-HRD1 ERAD-autophagy interplay maintains mitochondrial homeostasis in brown adipocytes.Proceedings of the National Academy of Sciences of the United States of America · 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

3 authors.

Shuangcheng Alivia WuDepartment of Molecular Physiology and Biological Physics, University of Virginia, School of Medicine, Charlottesville, VA 22903, USA. Electronic address: Shuangcheng.Wu@utsouthwestern.edu.
Zexin Jason LiDepartment of Molecular Physiology and Biological Physics, University of Virginia, School of Medicine, Charlottesville, VA 22903, USA; Medical Scientist Training Program, University of Virginia, School of Medicine, Charlottesville, VA 22903, USA. Electronic address: uqc4qj@virginia.edu.
Ling QiDepartment of Molecular Physiology and Biological Physics, University of Virginia, School of Medicine, Charlottesville, VA 22903, USA. Electronic address: xvr2hm@virginia.edu.

Funding

Secretory Pathway Protein Degradation Maintains Insulin Biogenesis + SecretionR01DK111174 · NIDDK · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI ARVAN, PETER, QI, LING · 2016 to 2024
$5.5M
Novel Role of Hepatic SEL1L-HRD1 ERAD in FGF21 Gene TranscriptionR01DK120330 · NIDDK · UNIVERSITY OF VIRGINIA · PI Deyu Fang, Ling Qi · 2018 to 2026
$4.9M
ERAD-STING Crosstalk in Microglia: Unraveling the Pathogenesis of Alzheimer's DiseaseR01AG089640 · NIA · UNIVERSITY OF VIRGINIA · PI Ling Qi, Zhen Zhao · 2024 to 2026
$4.1M
Regulation of Mitochondrial Dynamics by ERAD: Administrative SupplementR35GM130292 · NIGMS · UNIVERSITY OF VIRGINIA · PI QI, LING · 2019 to 2023
$2.5M
Mechanisms of ER-Protein Quality Control in PodocytesR01DK132786 · NIDDK · UNIVERSITY OF VIRGINIA · PI Ling Qi · 2023 to 2026
$1.6M
A TIMEM252-dependent Microvascular Endophenotype in Alzheimer’s DiseaseR01NS122060 · NINDS · UNIVERSITY OF SOUTHERN CALIFORNIA · PI ZHAO, ZHEN · 2024 to 2025
$1.5M
Mechanisms Underlying the Pathogenesis of SEL1L-HRD1 ERAD Disease VariantsR01NS138119 · NINDS · UNIVERSITY OF VIRGINIA · PI Ling Qi, Shengyi Sun · 2025 to 2026
$1.3M
A central role of SEL1L-HRD1 ERAD in LPL maturation in adipocytesR01DK137794 · NIDDK · UNIVERSITY OF VIRGINIA · PI Ling Qi · 2024 to 2026
$1.2M
NIA NIH HHS R01 AG089640NIDDK NIH HHS R01 DK111174NIDDK NIH HHS R01 DK120330NIDDK NIH HHS R01 DK132786NIDDK NIH HHS R01 DK137794NIGMS NIH HHS R35 GM130292NINDS NIH HHS R01 NS122060NINDS NIH HHS R01 NS138119
6 · The paper itself

Abstract

Protein misfolding and aggregation in the endoplasmic reticulum (ER) have been causally linked to a variety of human diseases. Two key pathways for eliminating misfolded proteins and aggregates in the ER are ER-associated degradation (ERAD) and ER-phagy, respectively. While both pathways have been well characterized biochemically, our understanding of their physiological relevance and significance remains limited. In recent years, significant advances have been made, including the generation and characterization of various knockout and knockin mouse models, the identification of human disease-associated or -causing variants, and insights into the coordination between ERAD and autophagy in physiological contexts. In this review, we summarize these advancements, highlighting the key roles of a highly conserved suppressor of lin-12-like-hydroxymethyl glutaryl-coenzyme A reductase degradation 1 (SEL1L-HRD1) protein complex of ERAD and ER-phagy in health and disease.

Indexed as

AutophagyEndoplasmic ReticulumEndoplasmic Reticulum-Associated DegradationAnimalsHumansProteolysisdisease variantsER-associated protein degradation (ERAD)ER-phagyER-phagy receptorsSEL1L-HRD1substrates

Identifiers

PMID39909774
PMCPMC12227305

What OpenQuestion holds

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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.