Evidence map›Paper›PMID 8922375›Full record

ArticleThe Journal of cell biology1996

COPII vesicles derived from mammalian endoplasmic reticulum microsomes recruit COPI.

T Rowe, M Aridor, J M McCaffery, H Plutner, C Nuoffer, W E Balch

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 71 papers.

0numbers the graph read from it
0cells of the map it votes in
71citing papers in PubMed
6.7field-weighted citation impact, top 3% 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

71 citing papers in PubMed, 166 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Post-Translational Regulation of HMG CoA Reductase.Cold Spring Harbor perspectives in biology · 2022
    Review
  9. Article
  10. Article
  11. Article
  12. COPII-mediated trafficking at the ER/ERGIC interface.Traffic (Copenhagen, Denmark) · 2019
    Review
  13. Dimeric sorting code for concentrative cargo selection by the COPII coat.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

11 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.

T RoweDepartment of Cell Biology, The Scripps Research Institute, La Jolla, California 92037, USA.
M Aridor
J M McCaffery
H Plutner
C Nuoffer
W E Balch
Scripps Research Institute · US

Funding

ROLE OF RAB PROTEINS AND CA2+ IN VESICULAR TRANSPORTR01GM042336 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI BALCH, WILLIAM EDWARD · 1990 to 2011
$4.8M
NCI NIH HHS CA586689NIGMS NIH HHS GM42336
6 · The paper itself

Abstract

ER to Golgi transport requires the function of two distinct vesicle coat complexes, termed COPI (coatomer) and COPII, whose assembly is regulated by the small GTPases ADP-ribosylation factor 1 (ARF1) and Sar1, respectively. To address their individual roles in transport, we have developed a new assay using mammalian microsomes that reconstitute the formation of ER-derived vesicular carriers. Vesicles released from the ER were found to contain the cargo molecule vesicular stomatitis virus glycoprotein (VSV-G) and p58, an endogenous protein that continuously recycles between the ER and pre-Golgi intermediates. Cargo was efficiently sorted from resident ER proteins during vesicle formation in vitro. Export of VSV-G and p58 were found to be exclusively mediated by COPII. Subsequent movement of ER-derived carriers to the Golgi stack was blocked by a trans-dominant ARF1 mutant restricted to the GDP-bound state, which is known to prevent COPI recruitment. To establish the initial site of coatomer assembly after export from the ER, we immunoisolated the vesicular intermediates and tested their ability to recruit COPI. Vesicles bound coatomer in a physiological fashion requiring an ARF1-guanine nucleotide exchange activity. These results suggest that coat exchange is an early event preceding the targeting of ER-derived vesicles to pre-Golgi intermediates.

Indexed as

Monomeric GTP-Binding ProteinsSaccharomyces cerevisiae ProteinsADP-Ribosylation Factor 1ADP-Ribosylation FactorsAnimalsBiological TransportCarrier ProteinsCells, CulturedCoated VesiclesCoatomer ProteinEndoplasmic ReticulumGenetic Complementation TestGolgi ApparatusGTP-Binding ProteinsGuanosine DiphosphateImmunomagnetic SeparationADP-Ribosylation Factor 1ADP-Ribosylation FactorsCarrier ProteinsCoatomer ProteinGTP-Binding ProteinsGuanosine DiphosphateLamin B ReceptorMembrane ProteinsMonomeric GTP-Binding ProteinsReceptors, Cytoplasmic and NuclearSaccharomyces cerevisiae ProteinsSAR1 protein, S cerevisiaeVesicular Transport Proteins

Identifiers

PMID8922375
PMCPMC2133376
OpenAlexW2104360518

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.