Evidence map›Paper›PMID 28441135›Full record

ArticleeLife2017

Proteomic mapping of cytosol-facing outer mitochondrial and ER membranes in living human cells by proximity biotinylation.

Victoria Hung, Stephanie S Lam, Namrata D Udeshi, Tanya Svinkina, Gaelen Guzman, Vamsi K Mootha, Steven A Carr, Alice Y Ting

Erratum issuedAbstract read
In one paragraph

Article in eLife, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 229 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
229citing 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

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

  1. Stay in touch with the endoplasmic reticulum.Science China. Life sciences · 2024
    Pooled it
  2. Review
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  15. Phenotypic CRISPR screens identify NLRX1 as an essential activator of the human mitochondrial permeability transition.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  16. Article
  17. Review
  18. Article
  19. Excessive CabioRxiv : the preprint server for biology · 2026
    Article
  20. Article

169 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

8 authors.

Victoria Hung *Department of Chemistry, Massachusetts Institute of Technology, Cambridge, United States.ORCID http://orcid.org/0000-0003-3972-2820
Stephanie S Lam *Department of Chemistry, Massachusetts Institute of Technology, Cambridge, United States.ORCID http://orcid.org/0000-0002-2687-3470
Namrata D UdeshiBroad Institute of MIT and Harvard, Cambridge, United States.
Tanya SvinkinaBroad Institute of MIT and Harvard, Cambridge, United States.
Gaelen GuzmanBroad Institute of MIT and Harvard, Cambridge, United States.
Vamsi K MoothaBroad Institute of MIT and Harvard, Cambridge, United States.ORCID http://orcid.org/0000-0001-9924-642X
Steven A CarrBroad Institute of MIT and Harvard, Cambridge, United States.
Alice Y TingDepartment of Chemistry, Massachusetts Institute of Technology, Cambridge, United States.ORCID http://orcid.org/0000-0002-8277-5226

Funding

Characterization of the Mitochondrial ProteomeR01GM077465 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI MOOTHA, VAMSI KRISHNA · 2007 to 2016
$4.3M
Spatially-resolved proteomic mapping of living cellsR01CA186568 · NCI · STANFORD UNIVERSITY · PI TING, ALICE Y · 2013 to 2018
$3.3M
NCI NIH HHS R01 CA186568NIGMS NIH HHS R01 GM077465
6 · The paper itself

Abstract

The cytosol-facing membranes of cellular organelles contain proteins that enable signal transduction, regulation of morphology and trafficking, protein import and export, and other specialized processes. Discovery of these proteins by traditional biochemical fractionation can be plagued with contaminants and loss of key components. Using peroxidase-mediated proximity biotinylation, we captured and identified endogenous proteins on the outer mitochondrial membrane (OMM) and endoplasmic reticulum membrane (ERM) of living human fibroblasts. The proteomes of 137 and 634 proteins, respectively, are highly specific and highlight 94 potentially novel mitochondrial or ER proteins. Dataset intersection identified protein candidates potentially localized to mitochondria-ER contact sites. We found that one candidate, the tail-anchored, PDZ-domain-containing OMM protein SYNJ2BP, dramatically increases mitochondrial contacts with rough ER when overexpressed. Immunoprecipitation-mass spectrometry identified ribosome-binding protein 1 (RRBP1) as SYNJ2BP's ERM binding partner. Our results highlight the power of proximity biotinylation to yield insights into the molecular composition and function of intracellular membranes.

Indexed as

AnimalsBiotinylationChlorocebus aethiopsCOS CellsEndoplasmic ReticulumHEK293 CellsHeLa CellsHumansIntracellular MembranesMembrane ProteinsMitochondriaPeroxidaseProteomicsMembrane ProteinsPeroxidaseAPEX2biochemistrycell biologyhumanmicroscopymitochondria-associated membranemitochondria-ER junctionspromiscuous enzymatic labelingsubcellular regions

Identifiers

PMID28441135
PMCPMC5404927

What OpenQuestion holds

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Registered trials

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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.