Evidence map›Paper›PMID 10913182›Full record

ArticleMolecular and cellular biology2000

Separation of membrane trafficking and actin remodeling functions of ARF6 with an effector domain mutant.

O Al-Awar, H Radhakrishna, N N Powell, J G Donaldson

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
3.6field-weighted citation impact, top 7% 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

34 citing papers in PubMed, 80 citations in OpenAlex.

  1. Article
  2. The Recycling Endosome in Nerve Cell Development: One Rab to Rule Them All?Frontiers in cell and developmental biology · 2020
    Review
  3. ELMOD1 Stimulates ARF6-GTP Hydrolysis to Stabilize Apical Structures in Developing Vestibular Hair Cells.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2018
    Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Regulators and Effectors of Arf GTPases in Neutrophils.Journal of immunology research · 2015
    Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
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  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 2 institutions in 1 country.

O Al-AwarLaboratory of Cell Biology, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, Maryland 20892, USA.
H Radhakrishna
N N Powell
J G Donaldson
National Heart Lung and Blood Institute · USNational Institutes of Health · US

Funding

CELLULAR FUNCTION OF THE ADP-RIBOSYLATION FACTOR 6 GTP BINDING PROTEINZ01HL000517 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI DONALDSON, JULIE G · 1996 to 2008
$3.2M
Arf GTP-binding proteins and membrane trafficZIAHL000517 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI DONALDSON, JULIE G · 2009 to 2016
$2.6M
6 · The paper itself

Abstract

The ADP-ribosylation factor 6 (ARF6) GTPase has a dual function in cells, regulating membrane traffic and organizing cortical actin. ARF6 activation is required for recycling of the endosomal membrane back to the plasma membrane (PM) and also for ruffling at the PM induced by Rac. Additionally, ARF6 at the PM induces the formation of actin-containing protrusions. To identify sequences in ARF6 that are necessary for these distinct functions, we examined the behavior of a chimeric protein of ARF1 and ARF6. The 1-6 chimera (with the amino half of ARF1 and the carboxyl half of ARF6) localized like ARF6 in HeLa cells and moved between the endosome and PM, but it did not form protrusions, an ARF6 effector function. Two residues in the amino-terminal half of ARF6, Q37 and S38, when substituted into the 1-6 chimera allowed protrusion formation, whereas removal of these residues from ARF6 resulted in an inability to form protrusions. Interestingly, expression of 1-6 in cells selectively inhibited protrusions induced by wild-type ARF6 but had no effect on ARF6-regulated membrane movement or Rac-induced ruffling. Thus, we have uncoupled two functions of ARF6, one involved in membrane trafficking, which is necessary for Rac ruffling, and another involved in protrusion formation.

Indexed as

ActinsADP-Ribosylation Factor 6ADP-Ribosylation FactorsAmino Acid SequenceBiological TransportEndosomesFluorescent Antibody TechniqueHeLa CellsHumansMolecular Sequence DataMutationActinsADP-Ribosylation Factor 6ADP-Ribosylation FactorsARF6 protein, human

Identifiers

PMID10913182
PMCPMC86076
OpenAlexW2149150287

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.