Evidence map›Paper›PMID 8089173›Full record

ArticleThe Journal of cell biology1994

Guanine nucleotide dissociation inhibitor is essential for Rab1 function in budding from the endoplasmic reticulum and transport through the Golgi stack.

F Peter, C Nuoffer, S N Pind, W E Balch

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
4.1field-weighted citation impact, top 6% 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

24 citing papers in PubMed, 84 citations in OpenAlex.

  1. Article
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  4. Article
  5. Article
  6. Article
  7. Cholesterol controls lipid endocytosis through Rab11.Molecular biology of the cell · 2007
    Article
  8. Rabs and their effectors: achieving specificity in membrane traffic.Proceedings of the National Academy of Sciences of the United States of America · 2006
    Review
  9. Article
  10. The BAR domain proteins: molding membranes in fission, fusion, and phagy.Microbiology and molecular biology reviews : MMBR · 2006
    Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. The mechanism of Golgi segregation during mitosis is cell type-specific.Proceedings of the National Academy of Sciences of the United States of America · 1997
    Article
  17. Article
  18. 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 1 country.

F PeterDepartment of Cell Biology, Scripps Research Institute, La Jolla, California 92037.
C Nuoffer
S N Pind
W E Balch
Scripps Research Institute · US

Funding

VESICULAR TRAFFICKING OF THE EGF RECEPTORP01CA058689 · NCI · UNIVERSITY OF CALIFORNIA SAN DIEGO · PI BALCH, WILLIAM E · 1993 to 2002
$5.0M
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 NCI CA58689NIGMS NIH HHS GM 42336NIGMS NIH HHS NCI GM 58689
6 · The paper itself

Abstract

The small GTPase Rab1 is required for vesicular traffic from the ER to the cis-Golgi compartment, and for transport between the cis and medial compartments of the Golgi stack. In the present study, we examine the role of guanine nucleotide dissociation inhibitor (GDI) in regulating the function of Rab1 in the transport of vesicular stomatitis virus glycoprotein (VSV-G) in vitro. Incubation in the presence of excess GDI rapidly (t1/2 < 30 s) extracted Rab1 from membranes, inhibiting vesicle budding from the ER and sequential transport between the cis-, medial-, and trans-Golgi cisternae. These results demonstrate a direct role for GDI in the recycling of Rab proteins. Analysis of rat liver cytosol by gel filtration revealed that a major pool of Rab1 fractionates with a molecular mass of approximately 80 kD in the form of a GDI-Rab1 complex. When the GDI-Rab1 complex was depleted from cytosol by use of a Rab1-specific antibody, VSV-G failed to exit the ER. However, supplementation of depleted cytosol with a GDI-Rab1 complex prepared in vitro from recombinant forms of Rab1 and GDI efficiently restored export from the ER, and transport through the Golgi stack. These results provide evidence that a cytosolic GDI-Rab1 complex is required for the formation of non-clathrin-coated vesicles mediating transport through the secretory pathway.

Indexed as

Guanine Nucleotide Dissociation InhibitorsMembrane Glycoproteinsrab1 GTP-Binding ProteinsAnimalsBiological TransportCell Membrane PermeabilityCoatomer ProteinCytosolEndoplasmic ReticulumGolgi ApparatusGTP-Binding ProteinsGTP PhosphohydrolasesIn Vitro TechniquesLiverMicrotubule-Associated ProteinsMolecular WeightCoatomer ProteinGDP dissociation inhibitor 1G protein, vesicular stomatitis virusGTP-Binding ProteinsGTP PhosphohydrolasesGuanine Nucleotide Dissociation InhibitorsMembrane GlycoproteinsMicrotubule-Associated ProteinsRAB1B protein, ratrab1 GTP-Binding ProteinsRecombinant ProteinsViral Envelope Proteins

Identifiers

PMID8089173
PMCPMC2290957
OpenAlexW2001582422

What OpenQuestion holds

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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.