Evidence map›Paper›PMID 27413010›Full record

ArticleMolecular biology of the cell2016

Sec24C/D-isoform-specific sorting of the preassembled ER-Golgi Q-SNARE complex.

Frank Adolf, Manuel Rhiel, Ingeborg Reckmann, Felix T Wieland

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
2.7field-weighted citation impact, top 11% 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

21 citing papers in PubMed, 38 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Nlp-dependent ER-to-Golgi transport.International journal of biological sciences · 2024
    Article
  5. Review
  6. Article
  7. 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
  8. Review
  9. Frontiers in immunology · 2022
    Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Review
  16. Trafficking of the amino acid transporter BBiochimica et biophysica acta. Molecular cell research · 2019
    Article
  17. Review
  18. The Journal of cell biology · 2017
    Article
  19. Article
  20. Article
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

4 authors at 1 institution in 2 countries.

Frank AdolfHeidelberg University Biochemistry Center, Heidelberg University, 69120 Heidelberg, Germany Frank.adolf@bzh.uni-heidelberg.de felix.wieland@bzh.uni-heidelberg.de.
Manuel RhielHeidelberg University Biochemistry Center, Heidelberg University, 69120 Heidelberg, Germany.
Ingeborg ReckmannHeidelberg University Biochemistry Center, Heidelberg University, 69120 Heidelberg, Germany.
Felix T WielandHeidelberg University Biochemistry Center, Heidelberg University, 69120 Heidelberg, Germany Frank.adolf@bzh.uni-heidelberg.de felix.wieland@bzh.uni-heidelberg.de.
Heidelberg University · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Secretory proteins are exported from the endoplasmic reticulum in COPII vesicles. SNARE proteins-core machinery for membrane fusion-are incorporated into COPII vesicles by direct interaction with Sec24. Here we report a novel mechanism for sorting of the ER-Golgi Q-SNAREs into COPII vesicles. Different mammalian Sec24 isoforms recruit either the R-SNARE Sec22b or the Q-SNAREs Syntaxin5, GS27, and Bet1. Syntaxin5 is the only Q-SNARE that directly interacts with Sec24C, requiring its "open" conformation. Mutation within the IxM cargo-binding site of Sec24C led to a drastic reduction in sorting of all three Q-SNAREs into COPII vesicles, implying their ER export as a preassembled complex. Analysis of immunoisolated COPII vesicles and intracellular localization of Sec24 isoforms indicate that all ER-Golgi SNAREs are present on the same vesicle. Combined with existing data, our findings yield a general concept of how Sec24 isoforms can recruit fusogenic SNARE subunits to keep them functionally apart and thus prime mammalian COPII vesicles for homotypic fusion.

Indexed as

Binding SitesCOP-Coated VesiclesEndoplasmic ReticulumGolgi ApparatusMembrane FusionMembrane ProteinsProtein BindingProtein IsoformsProtein TransportQ-SNARE ProteinsR-SNARE ProteinsSNARE ProteinsVesicular Transport ProteinsMembrane ProteinsProtein IsoformsQ-SNARE ProteinsR-SNARE ProteinsSEC24A protein, humanSEC24B protein, humanSNARE ProteinsVesicular Transport Proteins

Identifiers

PMID27413010
PMCPMC5007090
OpenAlexW2465192371

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.