Evidence map›Paper›PMID 37931956›Full record

ArticleLife science alliance2024

ESYT1 tethers the ER to mitochondria and is required for mitochondrial lipid and calcium homeostasis.

Alexandre Janer, Jordan L Morris, Michiel Krols, Hana Antonicka, Mari J Aaltonen, Zhen-Yuan Lin, Hanish Anand, Anne-Claude Gingras, Julien Prudent, Eric A Shoubridge

Open access · goldAbstract read
In one paragraph

Article in Life science alliance, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed, 1 pooled it
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

15 citing papers in PubMed, 1 synthesis or guideline pooled it, 20 citations in OpenAlex.

  1. Pooled it
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  13. Unlocking TRPM7 interactions: A database-driven quest.Computational and structural biotechnology journal · 2025
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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 3 institutions in 3 countries.

Alexandre JanerDepartment of Human Genetics, McGill University, Montreal, Canada.ORCID https://orcid.org/0000-0001-7421-3373
Jordan L MorrisMedical Research Council Mitochondrial Biology Unit, University of Cambridge, Cambridge, UK.
Michiel KrolsMontreal Neurological Institute, McGill University, Montreal, Canada.
Hana AntonickaDepartment of Human Genetics, McGill University, Montreal, Canada.ORCID https://orcid.org/0000-0002-2525-2867
Mari J AaltonenDepartment of Human Genetics, McGill University, Montreal, Canada.ORCID https://orcid.org/0000-0002-7333-9334
Zhen-Yuan LinLunenfeld-Tanenbaum Research Institute, Mount Sinai Hospital, Toronto, Canada.
Hanish AnandMedical Research Council Mitochondrial Biology Unit, University of Cambridge, Cambridge, UK.
Anne-Claude GingrasLunenfeld-Tanenbaum Research Institute, Mount Sinai Hospital, Toronto, Canada.ORCID https://orcid.org/0000-0002-6090-4437
Julien PrudentMedical Research Council Mitochondrial Biology Unit, University of Cambridge, Cambridge, UK.
Eric A ShoubridgeDepartment of Human Genetics, McGill University, Montreal, Canada eric.shoubridge@mcgill.ca.ORCID https://orcid.org/0000-0003-1498-9473
Montreal Neurological Institute and Hospital · CAUniversity of Cambridge · GBMount Sinai Hospital · CA

Funding

Medical Research Council MC_UU_00015/7
6 · The paper itself

Abstract

Mitochondria interact with the ER at structurally and functionally specialized membrane contact sites known as mitochondria-ER contact sites (MERCs). Combining proximity labelling (BioID), co-immunoprecipitation, confocal microscopy and subcellular fractionation, we found that the ER resident SMP-domain protein ESYT1 was enriched at MERCs, where it forms a complex with the outer mitochondrial membrane protein SYNJ2BP. BioID analyses using ER-targeted, outer mitochondrial membrane-targeted, and MERC-targeted baits, confirmed the presence of this complex at MERCs and the specificity of the interaction. Deletion of ESYT1 or SYNJ2BP reduced the number and length of MERCs. Loss of the ESYT1-SYNJ2BP complex impaired ER to mitochondria calcium flux and provoked a significant alteration of the mitochondrial lipidome, most prominently a reduction of cardiolipins and phosphatidylethanolamines. Both phenotypes were rescued by reexpression of WT ESYT1 and an artificial mitochondria-ER tether. Together, these results reveal a novel function for ESYT1 in mitochondrial and cellular homeostasis through its role in the regulation of MERCs.

Indexed as

CalciumEndoplasmic ReticulumMitochondriaSynaptotagminsHomeostasisLipidsCalciumLipidsSynaptotagmins

Identifiers

PMID37931956
PMCPMC10627786
OpenAlexW4388410197

What OpenQuestion holds

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LicenceCC BY
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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.