Evidence map›Paper›PMID 28430047›Full record

ReviewSmall GTPases2019

Arf GAPs and molecular motors.

Ruibai Luo, Christine E Reed, Jeffrey A Sload, Linda Wordeman, Paul A Randazzo, Pei-Wen Chen

Open access · bronzeAbstract readReviewVideo-Audio Media
In one paragraph

Review in Small GTPases, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
0.6field-weighted citation impact, top 35% 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

8 citing papers in PubMed, 16 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Review
  7. Arf GAPs as Regulators of the Actin Cytoskeleton-An Update.International journal of molecular sciences · 2019
    Review
  8. 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

6 authors at 3 institutions in 1 country.

Ruibai Luoa Laboratory of Cellular and Molecular Biology , National Cancer Institute, National Institutes of Health , Bethesda , MD , USA.
Christine E Reedc Department of Biology , Williams College , Williamstown , MA , USA.ORCID 0000-0002-8873-9592
Jeffrey A Sloadc Department of Biology , Williams College , Williamstown , MA , USA.
Linda Wordemanb Department of Physiology and Biophysics , University of Washington School of Medicine , Seattle , WA , USA.ORCID 0000-0002-9444-0650
Paul A Randazzoa Laboratory of Cellular and Molecular Biology , National Cancer Institute, National Institutes of Health , Bethesda , MD , USA.
Pei-Wen Chenc Department of Biology , Williams College , Williamstown , MA , USA.ORCID 0000-0001-5102-9709
Williams College · USNational Institutes of Health · USUniversity of Washington · US

Funding

Regulation of ADP-ribosylation factorZIABC007365 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI RANDAZZO, PAUL A · 2009 to 2025
$27.9M
Microtubule Dynamics and Chromosome SegregationR01GM069429 · NIGMS · UNIVERSITY OF WASHINGTON · PI WORDEMAN, LINDA · 2004 to 2020
$5.6M
NIGMS NIH HHS R01 GM069429
6 · The paper itself

Abstract

Arf GTPase-activating proteins (Arf GAPs) were first identified as regulators of the small GTP-binding proteins ADP-ribosylation factors (Arfs). The Arf GAPs are a large family of proteins in metazoans, outnumbering the Arfs that they regulate. The members of the Arf GAP family have complex domain structures and some have been implicated in particular cellular functions, such as cell migration, or with particular pathologies, such as tumor invasion and metastasis. The specific effects of Arfs sometimes depend on the Arf GAP involved in their regulation. These observations have led to speculation that the Arf GAPs themselves may affect cellular activities in capacities beyond the regulation of Arfs. Recently, 2 Arf GAPs, ASAP1 and AGAP1, have been found to bind directly to and influence the activity of myosins and kinesins, motor proteins associated with filamentous actin and microtubules, respectively. The Arf GAP-motor protein interaction is critical for cellular behaviors involving the actin cytoskeleton and microtubules, such as cell migration and other cell movements. Arfs, then, may function with molecular motors through Arf GAPs to regulate microtubule and actin remodeling.

Indexed as

Actin CytoskeletonAdaptor Proteins, Signal TransducingAnimalsCell MovementGTPase-Activating ProteinsHumansKinesinsMicrotubulesMyosinsProtein DomainsAdaptor Proteins, Signal TransducingAGAP1 protein, humanASAP1 protein, humanGTPase-Activating ProteinsKinesinsMyosinsADP-ribosylation factor GTPase-activating proteinADP-ribosylation factorsAGAP1ArfArf GAPASAP1Kif2Akinesin-13NM2Anonmuscle myosin 2A

Identifiers

PMID28430047
PMCPMC6548297
OpenAlexW2607328549

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.