Evidence map›Paper›PMID 32614697›Full record

ArticleMolecular biology of the cell2020

The ARF GAP ELMOD2 acts with different GTPases to regulate centrosomal microtubule nucleation and cytokinesis.

Rachel E Turn, Michael P East, Rytis Prekeris, Richard A Kahn

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
–field-weighted citation impact
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

10 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. γ-Tubulin in microtubule nucleation and beyond.Frontiers in cell and developmental biology · 2022
    Review
  9. Article
  10. Roles for ELMOD2 and Rootletin in ciliogenesis.Molecular biology of the cell · 2021
    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.

Rachel E TurnDepartment of Biochemistry, Emory University School of Medicine, Atlanta, GA 30322.
Michael P EastDepartment of Pharmacology, University of North Carolina Chapel Hill, Chapel Hill, NC 27599.
Rytis PrekerisDepartment of Cell and Developmental Biology, University of Colorado, Aurora, CO 80045.
Richard A KahnDepartment of Biochemistry, Emory University School of Medicine, Atlanta, GA 30322.ORCID 0000-0002-0259-0601

Funding

Molecular Mechanisms Regulating Epithelial Cell Apical Polarity and CiliogenesisR01DK064380 · NIDDK · UNIVERSITY OF COLORADO DENVER · PI Rytis Prekeris · 2004 to 2026
$7.1M
ENNCF - Viral Vector CoreP30NS055077 · NINDS · EMORY UNIVERSITY · PI LEVEY, ALLAN I · 2008 to 2018
$6.8M
Molecular mechanisms of ARF family GTPasesR35GM122568 · NIGMS · EMORY UNIVERSITY · PI KAHN, RICHARD A · 2017 to 2024
$3.7M
ELMOD2: proposed roles in regulating mitochondrial fusion and cell cycleF31CA236493 · NCI · EMORY UNIVERSITY · PI TURN, RACHEL ELIZABETH · 2019 to 2021
$137k
NCI NIH HHS F31 CA236493NIDDK NIH HHS R01 DK064380NIGMS NIH HHS R35 GM122568NINDS NIH HHS P30 NS055077
6 · The paper itself

Abstract

ELMOD2 is a ∼32 kDa protein first purified by its GTPase-activating protein (GAP) activity toward ARL2 and later shown to have uniquely broad specificity toward ARF family GTPases in in vitro assays. To begin the task of defining its functions in cells, we deleted ELMOD2 in immortalized mouse embryonic fibroblasts and discovered a number of cellular defects, which are reversed upon expression of ELMOD2-myc. We show that these defects, resulting from the loss of ELMOD2, are linked to two different pathways and two different GTPases: with ARL2 and TBCD to support microtubule nucleation from centrosomes and with ARF6 in cytokinesis. These data highlight key aspects of signaling by ARF family GAPs that contribute to previously underappreciated sources of complexity, including GAPs acting from multiple sites in cells, working with multiple GTPases, and contributing to the spatial and temporal control of regulatory GTPases by serving as both GAPs and effectors.

Indexed as

ADP-Ribosylation FactorsAnimalsCell Culture TechniquesCentrosomeCytokinesisCytoskeletal ProteinsFibroblastsGTPase-Activating ProteinsGTP-Binding ProteinsMiceMicrotubule-Associated ProteinsMicrotubulesMitochondriaMouse Embryonic Stem CellsADP-Ribosylation FactorsArl2 protein, mouseCytoskeletal ProteinsELMOD2 protein, mouseGTPase-Activating ProteinsGTP-Binding ProteinsMicrotubule-Associated Proteins

Identifiers

PMID32614697
PMCPMC7543072

What OpenQuestion holds

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LicenceCC BY-NC-SA
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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.