Evidence map›Paper›PMID 27531749›Full record

ArticleThe Journal of biological chemistry2016

Direct Functional Interaction of the Kinesin-13 Family Member Kinesin-like Protein 2A (Kif2A) and Arf GAP with GTP-binding Protein-like, Ankyrin Repeats and PH Domains1 (AGAP1).

Ruibai Luo, Pei-Wen Chen, Michael Wagenbach, Xiaoying Jian, Lisa Jenkins, Linda Wordeman, Paul A Randazzo

Erratum issuedOpen access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
1.9field-weighted citation impact, top 16% 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

1 citing paper in PubMed, 11 citations in OpenAlex.

  1. Arf GAPs and molecular motors.Small GTPases · 2019
    Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors at 3 institutions in 1 country.

Ruibai LuoFrom the Laboratory of Cellular and Molecular Biology and.
Pei-Wen ChenFrom the Laboratory of Cellular and Molecular Biology and.
Michael Wagenbachthe Department of Physiology and Biophysics, University of Washington School of Medicine, Seattle, Washington 98195.
Xiaoying JianFrom the Laboratory of Cellular and Molecular Biology and.
Lisa JenkinsLaboratory of Cell Biology, NCI, National Institutes of Health, Bethesda, Maryland 20892.
Linda Wordemanthe Department of Physiology and Biophysics, University of Washington School of Medicine, Seattle, Washington 98195.
Paul A RandazzoFrom the Laboratory of Cellular and Molecular Biology and randazzp@mail.nih.gov.
University of Washington · USGrinnell College · USNational Institutes of Health · US

Funding

CPTR - Mass Spectrometry UnitZICBC011430 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI JENKINS, LISA · 2012 to 2025
$9.4M
Microtubule Dynamics and Chromosome SegregationR01GM069429 · NIGMS · UNIVERSITY OF WASHINGTON · PI WORDEMAN, LINDA · 2004 to 2020
$5.6M
REGULATION OF ADP-RIBOSYLATION FACTORZ01BC007365 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI RANDAZZO, PAUL A · 1996 to 2008
$3.3M
Intramural NIH HHS Z01 BC007365NIGMS NIH HHS R01 GM069429
6 · The paper itself

Abstract

The molecular basis for control of the cytoskeleton by the Arf GTPase-activating protein AGAP1 has not been characterized. AGAP1 is composed of G-protein-like (GLD), pleckstrin homology (PH), Arf GAP, and ankyrin repeat domains. Kif2A was identified in screens for proteins that bind to AGAP1. The GLD and PH domains of AGAP1 bound the motor domain of Kif2A. Kif2A increased GAP activity of AGAP1, and a protein composed of the GLD and PH domains of AGAP1 increased ATPase activity of Kif2A. Knockdown (KD) of Kif2A or AGAP1 slowed cell migration and accelerated cell spreading. The effect of Kif2A KD on spreading could be rescued by expression of Kif2A-GFP or FLAG-AGAP1, but not by Kif2C-GFP. The effect of AGAP1 KD could be rescued by FLAG-AGAP1, but not by an AGAP1 mutant that did not bind Kif2A efficiently, ArfGAP1-HA or Kif2A-GFP. Taken together, the results support the hypothesis that the Kif2A·AGAP1 complex contributes to control of cytoskeleton remodeling involved in cell movement.

Indexed as

AnimalsCattleCells, CulturedGTPase-Activating ProteinsHeLa CellsHumansKinesinsAGAP1 protein, humanGTPase-Activating ProteinsKIF2A protein, humanKinesinsADP ribosylation factor (ARF)AGAP1Arf GTPase-activating proteincell biologyenzymeGTPase activating protein (GAP)Kif2Akinesinkinesin-13PH domainprotein complexsmall GTPase

Identifiers

PMID27531749
PMCPMC5076806
OpenAlexW2511055877

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.