Evidence map›Paper›PMID 11062263›Full record

ArticleThe Journal of cell biology2000

ACAPs are arf6 GTPase-activating proteins that function in the cell periphery.

T R Jackson, F D Brown, Z Nie, K Miura, L Foroni, J Sun, V W Hsu, J G Donaldson, P A Randazzo

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 86 papers.

0numbers the graph read from it
0cells of the map it votes in
86citing papers in PubMed
3.9field-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

86 citing papers in PubMed, 196 citations in OpenAlex.

  1. Article
  2. Article
  3. Akt-elicited phosphorylation of Acapin steers cell migration.Journal of molecular cell biology · 2025
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  7. Review
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  9. Cells · 2023
    Review
  10. Article
  11. Article
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  14. In vitro reconstitution reveals phosphoinositides as cargo-release factors and activators of the ARF6 GAP ADAP1.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. Article

26 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

9 authors at 5 institutions in 2 countries.

T R JacksonLaboratory of Cellular Oncology, Division of Basic Sciences, National Cancer Institute, Bethesda, Maryland 20892-4255, USA.
F D Brown
Z Nie
K Miura
L Foroni
J Sun
V W Hsu
J G Donaldson
P A Randazzo
National Cancer Institute · USBrigham and Women's Hospital · USNational Heart Lung and Blood Institute · USThe Royal Free Hospital · GBUniversity College London · GB

Funding

Regulation of ADP-ribosylation factorZIABC007365 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI RANDAZZO, PAUL A · 2009 to 2025
$27.9M
REGULATION OF ADP-RIBOSYLATION FACTORZ01BC007365 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI RANDAZZO, PAUL A · 1996 to 2008
$3.3M
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 GTP-binding protein ADP-ribosylation factor 6 (Arf6) regulates endosomal membrane trafficking and the actin cytoskeleton in the cell periphery. GTPase-activating proteins (GAPs) are critical regulators of Arf function, controlling the return of Arf to the inactive GDP-bound state. Here, we report the identification and characterization of two Arf6 GAPs, ACAP1 and ACAP2. Together with two previously described Arf GAPs, ASAP1 and PAP, they can be grouped into a protein family defined by several common structural motifs including coiled coil, pleckstrin homology, Arf GAP, and three complete ankyrin-repeat domains. All contain phosphoinositide-dependent GAP activity. ACAP1 and ACAP2 are widely expressed and occur together in the various cultured cell lines we examined. Similar to ASAP1, ACAP1 and ACAP2 were recruited to and, when overexpressed, inhibited the formation of platelet-derived growth factor (PDGF)-induced dorsal membrane ruffles in NIH 3T3 fibroblasts. However, in contrast with ASAP1, ACAP1 and ACAP2 functioned as Arf6 GAPs. In vitro, ACAP1 and ACAP2 preferred Arf6 as a substrate, rather than Arf1 and Arf5, more so than did ASAP1. In HeLa cells, overexpression of either ACAP blocked the formation of Arf6-dependent protrusions. In addition, ACAP1 and ACAP2 were recruited to peripheral, tubular membranes, where activation of Arf6 occurs to allow membrane recycling back to the plasma membrane. ASAP1 did not inhibit Arf6-dependent protrusions and was not recruited by Arf6 to tubular membranes. The additional effects of ASAP1 on PDGF-induced ruffling in fibroblasts suggest that multiple Arf GAPs function coordinately in the cell periphery.

Indexed as

3T3 CellsActinsADP-Ribosylation Factor 6ADP-Ribosylation FactorsAluminum CompoundsAmino Acid SequenceAmino Acid SubstitutionAnimalsArginineCarrier ProteinsCell MembraneCell Surface ExtensionsConserved SequenceCytoplasmCytoskeletonFluoridesACAP2 protein, mouseActinsADP-Ribosylation Factor 6ADP-Ribosylation FactorsAluminum Compoundsaluminum fluorideArf5 protein, mouseARF6 protein, humanArf6 protein, mouseArginineCarrier ProteinsFluoridesGTPase-Activating ProteinsGuanosine DiphosphatePhosphatidic AcidsPhosphatidylinositol 4,5-DiphosphatePlatelet-Derived Growth Factor

Identifiers

PMID11062263
PMCPMC2185579
OpenAlexW2086289346

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.