Evidence map›Paper›PMID 24616099›Full record

ArticleThe Journal of biological chemistry2014

Characterization of recombinant ELMOD (cell engulfment and motility domain) proteins as GTPase-activating proteins (GAPs) for ARF family GTPases.

Anna A Ivanova, Michael P East, Slee L Yi, Richard A Kahn

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
2.3field-weighted citation impact, top 13% 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

42 citing papers in PubMed, 56 citations in OpenAlex.

  1. Frontiers in immunology · 2025
    Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Review
  16. Roles for ELMOD2 and Rootletin in ciliogenesis.Molecular biology of the cell · 2021
    Article
  17. Article
  18. ARF family GTPases with links to cilia.American journal of physiology. Cell physiology · 2020
    Review
  19. Article
  20. Review
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 1 institution in 1 country.

Anna A IvanovaDepartment of Biochemistry, Emory University School of Medicine, Atlanta, Georgia 30322.
Michael P EastDepartment of Biochemistry, Emory University School of Medicine, Atlanta, Georgia 30322.
Slee L YiDepartment of Biochemistry, Emory University School of Medicine, Atlanta, Georgia 30322.
Richard A KahnDepartment of Biochemistry, Emory University School of Medicine, Atlanta, Georgia 30322. Electronic address: rkahn@emory.edu.
Emory University · US

Funding

NMR APPROACHES TO MEMBRANE ASSOCIATED ARF STRUCTURESR01GM061268 · NIGMS · UNIVERSITY OF GEORGIA (UGA) · PI PRESTEGARD, JAMES H. · 2000 to 2014
$2.9M
The Regulation and Cellular Activities of the ARL2 GTPaseR01GM090158 · NIGMS · EMORY UNIVERSITY · PI KAHN, RICHARD A · 2010 to 2017
$2.5M
Biology of the ARL13B GTPaseR01GM110663 · NIGMS · EMORY UNIVERSITY · PI CASPARY, TAMARA J., KAHN, RICHARD A · 2014 to 2017
$1.7M
NIGMS NIH HHS GM090158NIGMS NIH HHS GM61268NIGMS NIH HHS R01 GM061268NIGMS NIH HHS R01 GM090158NIGMS NIH HHS R01 GM110663
6 · The paper itself

Abstract

The ARF family of regulatory GTPases, within the RAS superfamily, is composed of ~30 members in mammals, including up to six ARF and at least 18 ARF-like (ARL) proteins. They exhibit significant structural and biochemical conservation and regulate a variety of essential cellular processes, including membrane traffic, cell division, and energy metabolism; each with links to human diseases. We previously identified members of the ELMOD family as GTPase-activating proteins (GAPs) for ARL2 that displayed crossover activity for ARFs as well. To further characterize the GAP activities of the three human ELMODs as GAPs we developed new preparations of each after overexpression in human embryonic kidney (HEK293T) cells. This allowed much higher specific activities and enhanced stability and solubility of the purified proteins. The specificities of ELMOD1-3 as GAPs for six different members of the ARF family were determined and found to display wide variations, which we believe will reveal differences in cellular functions of family members. The non-opioid sigma-1 receptor (S1R) was identified as a novel effector of GAP activity of ELMOD1-3 proteins as its direct binding to either ELMOD1 or ELMOD2 resulted in loss of GAP activity. These findings are critical to understand the roles of ELMOD proteins in cell signaling in general and in the inner ear specifically, and open the door to exploration of the regulation of their GAP activities via agonists or antagonists of the S1R.

Indexed as

ADP-Ribosylation FactorsCytoskeletal ProteinsGTPase-Activating ProteinsGTP-Binding ProteinsHEK293 CellsHumansReceptors, sigmaSigma-1 ReceptorADP-Ribosylation FactorsARL2 protein, humanCytoskeletal ProteinsELMOD1 protein, humanELMOD2 protein, humanELMOD3 protein, humanGTPase-Activating ProteinsGTP-Binding ProteinsReceptors, sigmaSigma-1 ReceptorARFARL2ELMODEnzyme KineticsGTPaseGTPase-activating Protein (GAP)HEK Cell ExpressionSigma-1 Receptor (S1R)Sigma ReceptorSignal Transduction

Identifiers

PMID24616099
PMCPMC4036250
OpenAlexW2030087337

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.