Evidence map›Paper›PMID 34133214›Full record

ArticleMolecular biology of the cell2021

VPS13D interacts with VCP/p97 and negatively regulates endoplasmic reticulum-mitochondria interactions.

Yuanjiao Du, Jingru Wang, Juan Xiong, Na Fang, Wei-Ke Ji

Open access · bronzeAbstract read
In one paragraph

Article in Molecular biology of the cell, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

21 citing papers in PubMed, 28 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

5 authors at 2 institutions in 1 country.

Yuanjiao DuDepartment of Biochemistry and Molecular Biology, School of Basic Medicine.
Jingru WangDepartment of Biochemistry and Molecular Biology, School of Basic Medicine.
Juan XiongDepartment of Anesthesiology, Tongji Hospital, Tongji Medical College, and.
Na FangDepartment of Biochemistry and Molecular Biology, School of Basic Medicine.
Wei-Ke JiDepartment of Biochemistry and Molecular Biology, School of Basic Medicine.
Huazhong University of Science and Technology · CNTongji Hospital · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Membrane contact sites (MCSs) between the endoplasmic reticulum (ER) and mitochondria are emerging as critical hubs for diverse cellular events, and alterations in the extent of these contacts are linked to neurodegenerative diseases. However, the mechanisms that control ER-mitochondria interactions are so far elusive. Here, we demonstrate a key role of vacuolar protein sorting-associated protein 13D (VPS13D) in the negative regulation of ER-mitochondria MCSs. VPS13D suppression results in extensive ER-mitochondria tethering, a phenotype that can be substantially rescued by suppression of the tethering proteins VAPB and PTPIP51. VPS13D interacts with valosin-containing protein (VCP/p97) to control the level of ER-resident VAPB at contacts. VPS13D is required for the stability of p97. Functionally, VPS13D suppression leads to severe defects in mitochondrial morphology, mitochondrial cellular distribution, and mitochondrial DNA synthesis. Together, our results suggest that VPS13D negatively regulates the ER-mitochondria MCSs, partially through its interactions with VCP/p97.

Indexed as

AnimalsCell Line, TumorChlorocebus aethiopsCOS CellsDNA, MitochondrialEndoplasmic ReticulumHEK293 CellsHeLa CellsHumansMitochondriaProteinsValosin Containing ProteinDNA, MitochondrialProteinsValosin Containing ProteinVCP protein, humanVPS13D protein, human

Identifiers

PMID34133214
PMCPMC8351740
OpenAlexW3170821373

What OpenQuestion holds

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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.