Evidence map›Paper›PMID 25202031›Full record

ArticleThe Journal of cell biology2014

Concentration of Sec12 at ER exit sites via interaction with cTAGE5 is required for collagen export.

Kota Saito, Koh Yamashiro, Noriko Shimazu, Tomoya Tanabe, Kenji Kontani, Toshiaki Katada

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 67 papers.

0numbers the graph read from it
0cells of the map it votes in
67citing 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

67 citing papers in PubMed, 109 citations in OpenAlex.

  1. Backbone and side chainBiomolecular NMR assignments · 2026
    Article
  2. Article
  3. Review
  4. Review
  5. Review
  6. Article
  7. Article
  8. Review
  9. [Research progress on collagen secretion mechanisms in scarring].Zhejiang da xue xue bao. Yi xue ban = Journal of Zhejiang University. Medical sciences · 2025
    Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. ER exit in physiology and disease.Frontiers in molecular biosciences · 2024
    Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Sorting and Export of Proteins at the Endoplasmic Reticulum.Cold Spring Harbor perspectives in biology · 2023
    Review
  20. Article

7 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 at 1 institution in 1 country.

Kota SaitoDepartment of Physiological Chemistry, Graduate School of Pharmaceutical Sciences, University of Tokyo, Bunkyo-ku, Tokyo 113-0033, Japan ksaito@mol.f.u-tokyo.ac.jp.
Koh YamashiroDepartment of Physiological Chemistry, Graduate School of Pharmaceutical Sciences, University of Tokyo, Bunkyo-ku, Tokyo 113-0033, Japan.
Noriko ShimazuDepartment of Physiological Chemistry, Graduate School of Pharmaceutical Sciences, University of Tokyo, Bunkyo-ku, Tokyo 113-0033, Japan.
Tomoya TanabeDepartment of Physiological Chemistry, Graduate School of Pharmaceutical Sciences, University of Tokyo, Bunkyo-ku, Tokyo 113-0033, Japan.
Kenji KontaniDepartment of Physiological Chemistry, Graduate School of Pharmaceutical Sciences, University of Tokyo, Bunkyo-ku, Tokyo 113-0033, Japan.
Toshiaki KatadaDepartment of Physiological Chemistry, Graduate School of Pharmaceutical Sciences, University of Tokyo, Bunkyo-ku, Tokyo 113-0033, Japan.
The University of Tokyo · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Mechanisms for exporting variably sized cargo from the endoplasmic reticulum (ER) using the same machinery remain poorly understood. COPII-coated vesicles, which transport secretory proteins from the ER to the Golgi apparatus, are typically 60-90 nm in diameter. However, collagen, which forms a trimeric structure that is too large to be accommodated by conventional transport vesicles, is also known to be secreted via a COPII-dependent process. In this paper, we show that Sec12, a guanine-nucleotide exchange factor for Sar1 guanosine triphosphatase, is concentrated at ER exit sites and that this concentration of Sec12 is specifically required for the secretion of collagen VII but not other proteins. Furthermore, Sec12 recruitment to ER exit sites is organized by its direct interaction with cTAGE5, a previously characterized collagen cargo receptor component, which functions together with TANGO1 at ER exit sites. These findings suggest that the export of large cargo requires high levels of guanosine triphosphate-bound Sar1 generated by Sec12 localized at ER exit sites.

Indexed as

AnimalsAntigens, NeoplasmAryl Hydrocarbon Receptor Nuclear TranslocatorCell Line, TumorCollagen Type VIICOP-Coated VesiclesDNA-Binding ProteinsEndoplasmic ReticulumFemaleGolgi ApparatusGuanine Nucleotide Exchange FactorsGuanosine TriphosphateHEK293 CellsHeLa CellsHumansJurkat CellsAntigens, NeoplasmARNT protein, humanAryl Hydrocarbon Receptor Nuclear TranslocatorCollagen Type VIIDNA-Binding ProteinsGuanine Nucleotide Exchange FactorsGuanosine TriphosphateMIA2 protein, humanMonomeric GTP-Binding ProteinsNeoplasm ProteinsPREB protein, humanRNA, Small InterferingSAR1A protein, humanSEC16A protein, humanTranscription FactorsVesicular Transport Proteins

Identifiers

PMID25202031
PMCPMC4164946
OpenAlexW2066454786

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.