Evidence map›Paper›PMID 20214751›Full record

ArticleTraffic (Copenhagen, Denmark)2010

Modifications to the C-terminus of Arf1 alter cell functions and protein interactions.

Xiaoying Jian, Margaret Cavenagh, James M Gruschus, Paul A Randazzo, Richard A Kahn

Open access · bronzeAbstract read
In one paragraph

Article in Traffic (Copenhagen, Denmark), 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
2.5field-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

39 citing papers in PubMed, 55 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Exomer complex regulates protein traffic at the TGN through differential interactions with cargos and clathrin adaptor complexes.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2021
    Article
  7. ARF family GTPases with links to cilia.American journal of physiology. Cell physiology · 2020
    Review
  8. Review
  9. Article
  10. Article
  11. Multiple interactions between an Arf/GEF complex and charged lipids determine activation kinetics on the membrane.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  12. Article
  13. Article
  14. mBio · 2017
    Article
  15. Pex35 is a regulator of peroxisome abundance.Journal of cell science · 2017
    Article
  16. Article
  17. Inhibition of Cytohesins Protects against Genetic Models of Motor Neuron Disease.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2015
    Article
  18. Article
  19. Article
  20. Review
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 3 institutions in 1 country.

Xiaoying JianLaboratory of Cellular and Molecular Biology, National Cancer Institute, Bldg 37 Room 2042, Bethesda, MD 20892, USA.
Margaret Cavenagh
James M Gruschus
Paul A Randazzo
Richard A Kahn
National Cancer Institute · USEmory University · USNational Institutes of Health · US

Funding

Regulation of ADP-ribosylation factorZIABC007365 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI RANDAZZO, PAUL A · 2009 to 2025
$27.9M
NMR APPROACHES TO MEMBRANE ASSOCIATED ARF STRUCTURESR01GM061268 · NIGMS · UNIVERSITY OF GEORGIA (UGA) · PI PRESTEGARD, JAMES H. · 2000 to 2014
$2.9M
The Regulation and Cellular Activities of the ARL2 GTPaseR01GM090158 · NIGMS · EMORY UNIVERSITY · PI KAHN, RICHARD A · 2010 to 2017
$2.5M
Regulation of vesicular membrane traffic by ARF proteinsR01GM067226 · NIGMS · EMORY UNIVERSITY · PI KAHN, RICHARD A · 2003 to 2011
$2.3M
Intramural NIH HHS ZIA BC007365NIGMS NIH HHS GM-61268NIGMS NIH HHS GM-67226NIGMS NIH HHS R01 GM061268NIGMS NIH HHS R01 GM067226NIGMS NIH HHS R01 GM090158
6 · The paper itself

Abstract

Arf family proteins are approximately 21-kDa GTP-binding proteins that are critical regulators of membrane traffic and the actin cytoskeleton. Studies examining the complex signaling pathways underlying Arf action have relied on recombinant proteins comprised of Arf fused to epitope tags or proteins, such as glutathione S-transferase or green fluorescent protein, for both cell-based mammalian cell studies and bacterially expressed recombinant proteins for biochemical assays. However, the effects of such protein fusions on the biochemical properties relevant to the cellular function have been only incompletely studied at best. Here, we have characterized the effect of C-terminal tagging of Arf1 on (i) function in Saccharomyces cerevisiae, (ii) in vitro nucleotide exchange and (iii) interaction with guanine nucleotide exchange factors and GTPase-activating proteins. We found that the tagged Arfs were substantially impaired or altered in each assay, compared with the wild-type protein, and these changes are certain to alter actions in cells. We discuss the results related to the interpretation of experiments using these reagents and we propose that authors and editors consistently adopt a few simple rules for describing and discussing results obtained with Arf family members that can be readily applied to other proteins.

Indexed as

ADP-Ribosylation Factor 1Cell LineEpitopesGlutathione TransferaseGreen Fluorescent ProteinsGTPase-Activating ProteinsGTP-Binding ProteinsHumansModels, BiologicalModels, MolecularProteinsProtein Structure, SecondaryProtein Structure, TertiaryRecombinant ProteinsSaccharomyces cerevisiaeADP-Ribosylation Factor 1EpitopesGlutathione TransferaseGreen Fluorescent ProteinsGTPase-Activating ProteinsGTP-Binding ProteinsProteinsRecombinant Proteins

Identifiers

PMID20214751
PMCPMC2874613
OpenAlexW2156203087

What OpenQuestion holds

Textmetadata
LicenceTDM
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.