Evidence map›Paper›PMID 26283797›Full record

ArticleThe Journal of cell biology2015

Mdm1/Snx13 is a novel ER-endolysosomal interorganelle tethering protein.

W Mike Henne, Lu Zhu, Zsolt Balogi, Christopher Stefan, Jeffrey A Pleiss, Scott D Emr

Abstract read
In one paragraph

Article in The Journal of cell biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 88 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
88citing papers in PubMed, 1 pooled it
–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

88 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Pooled it
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  5. Heterogeneity, dynamics and organelle interactions of lipid droplets.Nature reviews. Molecular cell biology · 2026
    Review
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28 more citing papers are in PubMed but not listed here.

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

6 authors.

W Mike HenneDepartment of Cell Biology, University of Texas Southwestern Medical Center, Dallas, TX 75390 Mike.Henne@utsouthwestern.edu sde26@cornell.edu.
Lu ZhuDepartment of Molecular Biology and Genetics, Cornell University, Ithaca, NY 14853 Weill Institute for Cell and Molecular Biology, Cornell University, Ithaca, NY 14853.
Zsolt BalogiDepartment of Molecular Biology and Genetics, Cornell University, Ithaca, NY 14853 Weill Institute for Cell and Molecular Biology, Cornell University, Ithaca, NY 14853.
Christopher StefanMedical Research Council Laboratory for Molecular Cell Biology, University College London, London WC1E 6BT, England, UK.
Jeffrey A PleissDepartment of Molecular Biology and Genetics, Cornell University, Ithaca, NY 14853.
Scott D EmrDepartment of Molecular Biology and Genetics, Cornell University, Ithaca, NY 14853 Weill Institute for Cell and Molecular Biology, Cornell University, Ithaca, NY 14853 Mike.Henne@utsouthwestern.edu sde26@cornell.edu.

Funding

Medical Research Council MC_UU_12018/6
6 · The paper itself

Abstract

Although endolysosomal trafficking is well defined, how it is regulated and coordinates with cellular metabolism is unclear. To identify genes governing endolysosomal dynamics, we conducted a global fluorescence-based screen to reveal endomembrane effector genes. Screening implicated Phox (PX) domain-containing protein Mdm1 in endomembrane dynamics. Surprisingly, we demonstrate that Mdm1 is a novel interorganelle tethering protein that localizes to endoplasmic reticulum (ER)-vacuole/lysosome membrane contact sites (MCSs). We show that Mdm1 is ER anchored and contacts the vacuole surface in trans via its lipid-binding PX domain. Strikingly, overexpression of Mdm1 induced ER-vacuole hypertethering, underscoring its role as an interorganelle tether. We also show that Mdm1 and its paralogue Ydr179w-a (named Nvj3 in this study) localize to ER-vacuole MCSs independently of established tether Nvj1. Finally, we find that Mdm1 truncations analogous to neurological disease-associated SNX14 alleles fail to tether the ER and vacuole and perturb sphingolipid metabolism. Our work suggests that human Mdm1 homologues may play previously unappreciated roles in interorganelle communication and lipid metabolism.

Indexed as

Binding SitesEndoplasmic ReticulumEndosomesIntermediate Filament ProteinsLysosomesProtein BindingProtein Structure, TertiaryProtein TransportSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSphingolipidsVacuolesIntermediate Filament ProteinsMDM1 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsSphingolipids

Identifiers

PMID26283797
PMCPMC4539980

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.