CoChat
Sign Up
Cited by 1,275Mitochondrial Function and PathologyCellular transport and secretionIon Channels and Receptors

An ER-Mitochondria Tethering Complex Revealed by a Synthetic Biology Screen

Open access
Kornmann, Benoît, Currie, Erin, Collins, Sean R., Schuldiner, Maya, Nunnari, Jodi, Weissman, Jonathan S., Walter, Peter·2009·Science
DOI 10.1126/science.1175088PMC PMC2933203
Open this paper in CoChat — free account

Abstract

Making Connections: Endoplasmic reticulum (ER)–mitochondria connections have been implicated in many physiological processes, including calcium homeostasis, signaling, membrane biogenesis, and apoptosis. Kornmann et al. (p. 477 , published online 25 June; see the Perspective by Wiedemann et al. ) looked for a proteinaceous link between the ER and mitochondria and, using combinations of synthetic biology and classical yeast genetics, found a protein complex that tethers the two organelles. A large-scale genetic interaction map suggests that these ER-mitochondria connections are important for interorganellar phospholipid exchange.

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Integrity signals

Registry

Crossref · 10.1126/science.1175088

Cites

32 of 32 references verified0 citation errors · 0 not checkable

Statistics

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

  • The ERMES complex is composed of four core subunits: an ER-resident protein Mmm1, a cytosolic protein Mdm12, and mitochondrial outer membrane proteins Mdm10 and Mdm34.

    “The ERMES complex is composed of four core subunits: an ER-resident protein Mmm1, a cytosolic protein Mdm12, and mitochondrial outer membrane proteins Mdm10 and Mdm34 [21] (Figure 1A).”

    From In Candida glabrata, ERMES Component GEM1 Controls Mitochondrial Morphology, mtROS, and Drug Efflux Pump Expression, Resulting in Azole Susceptibility (2023) · cites this paper as [21]

    The paper identifies Mmm1, Mdm10, Mdm12, and Mdm34 as ERMES components and places Mmm1 at the ER and Mdm10 and Mdm34 at the mitochondrial outer membrane. It describes Mdm12 as a peripheral outer mitochondrial membrane protein whose localization depends on interaction partners, rather than identifying it as a cytosolic protein. The relevant passages are labeled “Abstract” in our copy; no page number is available. (LLM, conf=0.87)

    Experimental — accuracy not yet measured

  • MDM34 encodes a protein of the mitochondrial outer membrane that is part of the ERMES complex, which tethers mitochondria to the ER and is also involved in their contact with peroxisomes.

    “MDM34 encodes a protein of the mitochondrial outer membrane that is a part of the ERMES complex that tethers mitochondria to the ER and is also involved in their contact with peroxisomes (Kornmann et al. 2009; Cohen et al. 2014).”

    From Mitochondrial retrograde control of transcription evolves with respiratory stress, metabolic adaptation, and virulence in budding yeasts (2026) · cites this paper as Kornmann et al. 2009

    The supplied passages (labeled Abstract; no page given) identify Mdm34 as an outer mitochondrial membrane protein and a component of ERMES, which connects the ER and mitochondria. Our copy does not address ERMES or Mdm34 involvement in contacts with peroxisomes (also searched: peroxisome), so that part of the sentence is not supported by this source. (LLM, conf=0.88)

    Experimental — accuracy not yet measured

  • Deletion of any four proteins of the ERMES core complex results in impaired formation of the ERMES complex and instability of ER-mitochondrial contact.

    “Deletion of any four proteins of the ERMES core complex results in the impaired formation of the ERMES complex and instability of ER-mitochondrial contact [21].”

    From In Candida glabrata, ERMES Component GEM1 Controls Mitochondrial Morphology, mtROS, and Drug Efflux Pump Expression, Resulting in Azole Susceptibility (2023) · cites this paper as [21]

  • In Saccharomyces cerevisiae, the outer mitochondrial membrane is connected to the endoplasmic reticulum through the contact site formed by the ER-mitochondria encounter structure (ERMES) complex.

    “In Saccharomyces cerevisiae, the outer mitochondrial membrane is connected to the endoplasmic reticulum (ER) through the contact site formed by the ER-mitochondria encounter structure (ERMES) complex [21].”

    From In Candida glabrata, ERMES Component GEM1 Controls Mitochondrial Morphology, mtROS, and Drug Efflux Pump Expression, Resulting in Azole Susceptibility (2023) · cites this paper as [21]

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Cites

Flagged first, then by citations

Research works printed but not linked: 2

  1. [20]Kondo-Okamoto N Shaw JM Okamoto K J Biol Chem 278 48997 2003 12972421
  2. [28]Birner R Bürgermeister M Schneiter R Daum G Mol Biol Cell 12 997 2001 11294902 PMC32282

Cited by

Sorted by citations

Related

Authors
Kornmann, B., Currie, E., Collins, S. R., Schuldiner, M., Nunnari, J., Weissman, J. S., & Walter, P.
Affiliations
  • Department of Biochemistry and Biophysics, University of California at San Francisco, San Francisco, CA 94158, USA.
  • University of California, San Francisco (US)
  • Howard Hughes Medical Institute (US)
  • Weizmann Institute of Science (IL)
  • University of California, Davis (US)
Corresponding author
  • Currie, Erin
  • Collins, Sean R.
ORCID
Venue
Science
Publisher
American Association for the Advancement of Science (AAAS)
Published
2009-07-24
Volume
325
Issue
5939
Pages
477-481
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
DOI
10.1126/science.1175088
PMC
PMC2933203
OpenAlex
W1997527771
Cited by
1,275
References
32
Citations by year
2026: 29 · 2025: 49 · 2024: 79 · 2023: 54 · 2022: 63 · 2021: 91 · 2020: 86 · 2019: 89 · 2018: 80 · 2017: 85 · 2016: 90 · 2015: 74 · 2014: 91 · 2013: 88 · 2012: 73
FWCI
30.30
Type
journal article
Language
en
Open access
Locations
  • Science (publishedVersion)
  • PubMed (publishedVersion)
  • PubMed Central (acceptedVersion)
Funders
  • National Science Foundation
  • Howard Hughes Medical Institute
  • Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung
  • National Institutes of Health
  • National Institute of General Medical Sciences (R01GM062942, R01GM032384)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
  • Life Sciences › Neuroscience › Sensory Systems › Ion Channels and Receptors
Keywords
ER-mitochondria tethering, inter-organelle communication, phospholipid synthesis, calcium signaling, genetic interaction mapping
MeSH terms
Animals, Endoplasmic Reticulum, Membrane Proteins, Mitochondria, Phospholipids, Recombinant Fusion Proteins, Saccharomyces cerevisiae, Calcium Signaling, Mitochondrial Proteins, Saccharomyces cerevisiae Proteins, Mice

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review