Evidence map›Paper›PMID 9050849›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1997

Cytohesin-1, a cytosolic guanine nucleotide-exchange protein for ADP-ribosylation factor.

E Meacci, S C Tsai, R Adamik, J Moss, M Vaughan

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
11.8field-weighted citation impact, top 1% 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

41 citing papers in PubMed, 147 citations in OpenAlex.

  1. Article
  2. Physiological and Pathological Roles of the Cytohesin Family in Neurons.International journal of molecular sciences · 2022
    Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. FRMD4A regulates epithelial polarity by connecting Arf6 activation with the PAR complex.Proceedings of the National Academy of Sciences of the United States of America · 2010
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Cybr, a cytokine-inducible protein that binds cytohesin-1 and regulates its activity.Proceedings of the National Academy of Sciences of the United States of America · 2002
    Article
  16. Review
  17. Controlling small guanine-nucleotide-exchange factor function through cytoplasmic RNA intramers.Proceedings of the National Academy of Sciences of the United States of America · 2001
    Article
  18. ARF-GEP(100), a guanine nucleotide-exchange protein for ADP-ribosylation factor 6.Proceedings of the National Academy of Sciences of the United States of America · 2001
    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

5 authors at 2 institutions in 1 country.

E MeacciPulmonary-Critical Care Medicine Branch, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD 20892-1590, USA.
S C Tsai
R Adamik
J Moss
M Vaughan
National Heart Lung and Blood Institute · USNational Institutes of Health · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cytohesin-1, a protein abundant in cells of the immune system, has been proposed to be a human homolog of the Saccharomyces cerevisiae Sec7 gene product, which is crucial in protein transport. More recently, the same protein has been reported to be a regulatory factor for the alphaLbeta2 integrin in lymphocytes. Overexpression of human or yeast ADP-ribosylation factor (ARF) genes rescues yeast with Sec7 defects, restoring secretory pathway function. ARFs, 20-kDa guanine nucleotide-binding proteins initially identified by their ability to stimulate cholera toxin ADP-ribosyltransferase activity and now recognized as critical components in intracellular vesicular transport, exist in an inactive cytosolic form with GDP bound (ARF-GDP). Interaction with a guanine nucleotide-exchange protein (GEP) accelerates exchange of GDP for GTP, producing the active ARF-GTP. Both soluble and particulate GEPs have been described. To define better the interaction between ARF and Sec7-related proteins, effects of cytohesin-1, synthesized in Escherichia coli, on ARF activity were evaluated. Cytohesin-1 enhanced binding of 35S-labeled guanosine 5'-[gamma-thio]triphosphate [35S]GTP[gammaS] or [3H]GDP to ARF purified from bovine brain (i.e., it appeared to function as an ARF-GEP). Addition of cytohesin-1 to ARF3 with [35S]GTP[gammaS] bound, accelerated [35S]GTP[gammaS] release to a similar degree in the presence of unlabeled GDP or GTP[gammaS] and to a lesser degree with GDP[betaS]; release was negligible without added nucleotide. Cytohesin-1 also increased ARF1 binding to a Golgi fraction, but its effect was not inhibited by brefeldin A (BFA), a drug that reversibly inhibits Golgi function. In this regard, it differs from a recently reported BFA-sensitive ARF-GEP that contains a Sec7 domain.

Indexed as

Guanine Nucleotide Exchange FactorsADP-Ribosylation Factor 1ADP-Ribosylation FactorsAmino Acid SequenceBrefeldin ACell Adhesion MoleculesCell Line, TransformedCloning, MolecularCyclopentanesFungal ProteinsGenes, FungalGTP-Binding ProteinsGuanosine 5'-O-(3-Thiotriphosphate)Guanosine DiphosphateGuanosine TriphosphateHumansADP-Ribosylation Factor 1ADP-Ribosylation FactorsBrefeldin ACell Adhesion MoleculesCyclopentanescytohesin-1Fungal ProteinsGTP-Binding ProteinsGuanine Nucleotide Exchange FactorsGuanosine 5'-O-(3-Thiotriphosphate)Guanosine DiphosphateGuanosine TriphosphateSec7 guanine nucleotide exchange factors

Identifiers

PMID9050849
PMCPMC19987
OpenAlexW1969906851

What OpenQuestion holds

Textmetadata
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.