Evidence map›Paper›PMID 25619760›Full record

ArticleCurrent biology : CB2015

Sec24 is a coincidence detector that simultaneously binds two signals to drive ER export.

Silvere Pagant, Alexander Wu, Samuel Edwards, Frances Diehl, Elizabeth A Miller

Open access · bronzeAbstract read
In one paragraph

Article in Current biology : CB, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
4.7field-weighted citation impact, top 5% 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

42 citing papers in PubMed, 90 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Trafficking of the human NaProtein science : a publication of the Protein Society · 2026
    Article
  5. A class of COPI cargo receptors regulates processing of transmembrane proteins by reinforcing their Golgi retention.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  6. Review
  7. Review
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Trafficking of Connexin36 (Cx36) in the early secretory pathway.bioRxiv : the preprint server for biology · 2024
    Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Frontiers in microbiology · 2023
    Article
  19. Selective inhibition of protein secretion by abrogating receptor-coat interactions during ER export.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors at 1 institution in 1 country.

Silvere PagantDepartment of Biological Sciences, Columbia University, New York, NY 10027, USA. Electronic address: sp2430@columbia.edu.
Alexander WuDepartment of Biological Sciences, Columbia University, New York, NY 10027, USA.
Samuel EdwardsDepartment of Biological Sciences, Columbia University, New York, NY 10027, USA.
Frances DiehlDepartment of Biological Sciences, Columbia University, New York, NY 10027, USA.
Elizabeth A MillerDepartment of Biological Sciences, Columbia University, New York, NY 10027, USA. Electronic address: em2282@columbia.edu.
Columbia University · US

Funding

ER export and the quality control checkpoint during membrane protein biogenesisR01GM078186 · NIGMS · COLUMBIA UNIV NEW YORK MORNINGSIDE · PI BULINSKI, JEANNETTE CHLOE, MILLER, ELIZABETH A. · 2006 to 2015
$2.7M
Molecular mechanisms of cargo capture into ER-derived transport vesiclesR01GM085089 · NIGMS · COLUMBIA UNIV NEW YORK MORNINGSIDE · PI BULINSKI, JEANNETTE CHLOE, MILLER, ELIZABETH A. · 2008 to 2016
$2.4M
The role of copines in the regulation of the actin cytoskeleton and membrane traffickingR15GM078089 · NIGMS · CENTRAL MICHIGAN UNIVERSITY · PI CYNTHIA K DAMER · 2008 to 2026
$1.6M
NIGMS NIH HHS R01 GM078186NIGMS NIH HHS R01GM078186NIGMS NIH HHS R01 GM085089NIGMS NIH HHS R01GM085089NIGMS NIH HHS R15 GM078089
6 · The paper itself

Abstract

backgroundIncorporation of secretory proteins into ER-derived vesicles involves recognition of cytosolic signals by the COPII coat protein, Sec24. Additional cargo diversity is achieved through cargo receptors, which include the Erv14/Cornichon family that mediates export of transmembrane proteins despite the potential for such clients to directly interact with Sec24. The molecular function of Erv14 thus remains unclear, with possible roles in COPII binding, membrane domain chaperoning, and lipid organization.

resultsUsing a targeted mutagenesis approach to define the mechanism of Erv14 function, we identify conserved residues in the second transmembrane domain of Erv14 that mediate interaction with a subset of Erv14 clients. We further show that interaction of Erv14 with a novel cargo-binding surface on Sec24 is necessary for efficient trafficking of all of its clients. However, we also determine that some Erv14 clients also directly engage an adjacent cargo-binding domain of Sec24, suggesting a novel mode of dual interaction between cargo and coat.

conclusionsWe conclude that Erv14 functions as a canonical cargo receptor that couples membrane proteins to the COPII coat, but that maximal export requires a bivalent signal that derives from motifs on both the cargo protein and Erv14. Sec24 can thus be considered a coincidence detector that binds simultaneously to multiple signals to drive packaging of polytopic membrane proteins. This mode of dual signal binding to a single coat protein might serve as a general mechanism to trigger efficient capture, or may be specifically employed in ER export to control deployment of nascent proteins.

Indexed as

Endoplasmic ReticulumMembrane ProteinsProtein TransportSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsErv14 protein, S cerevisiaeMembrane ProteinsSaccharomyces cerevisiae ProteinsSEC24 protein, S cerevisiae

Identifiers

PMID25619760
PMCPMC4334704
OpenAlexW1996740572

What OpenQuestion holds

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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.