Evidence map›Paper›PMID 24040268›Full record

ArticlePloS one2013

Role of phosphatidylinositol 4,5-bisphosphate in regulating EHD2 plasma membrane localization.

Laura C Simone, Steve Caplan, Naava Naslavsky

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
2.0field-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

23 citing papers in PubMed, 32 citations in OpenAlex.

  1. Review
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  11. Cardiomyocyte damage control in heart failure and the role of the sarcolemma.Journal of muscle research and cell motility · 2019
    Article
  12. Review
  13. Article
  14. Article
  15. Low-Intensity Ultrasound Modulates CaAnnals of biomedical engineering · 2018
    Article
  16. Article
  17. Role of EHD2 in migration and invasion of human breast cancer cells.Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2015
    Article
  18. Review
  19. Article
  20. 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

3 authors at 1 institution in 1 country.

Laura C SimoneDepartment of Biochemistry and Molecular Biology and Eppley Cancer Center, University of Nebraska Medical Center, Omaha, Nebraska, United States of America.
Steve Caplan
Naava Naslavsky
University of Nebraska Medical Center · US

Funding

CHEMICAL CARCINOGENESIS &CANCER BIOLOGYT32CA009476 · NCI · UNIVERSITY OF NEBRASKA MEDICAL CENTER · PI Jennifer D. Black · 1988 to 2026
$6.2M
Molecular Mechanisms Controlling Endocytic RecyclingR01GM074876 · NIGMS · UNIVERSITY OF NEBRASKA MEDICAL CENTER · PI CAPLAN, STEVEN H · 2006 to 2015
$2.6M
Nebraska Center for Cellular SignalingP20GM103489 · NIGMS · UNIVERSITY OF NEBRASKA MEDICAL CENTER · PI JOHNSON, KEITH R · 2012 to 2012
$2.0M
NCI NIH HHS 5T32 CA009476-23NCI NIH HHS T32 CA009476NIGMS NIH HHS 5P20GM103489-10NIGMS NIH HHS P20 GM103489NIGMS NIH HHS R01 GM074876NIGMS NIH HHS R01GM074876
6 · The paper itself

Abstract

The four mammalian C-terminal Eps15 homology domain-containing proteins (EHD1-EHD4) play pivotal roles in endocytic membrane trafficking. While EHD1, EHD3 and EHD4 associate with intracellular tubular/vesicular membranes, EHD2 localizes to the inner leaflet of the plasma membrane. Currently, little is known about the regulation of EHD2. Thus, we sought to define the factors responsible for EHD2's association with the plasma membrane. The subcellular localization of endogenous EHD2 was examined in HeLa cells using confocal microscopy. Although EHD partner proteins typically mediate EHD membrane recruitment, EHD2 was targeted to the plasma membrane independent of two well-characterized binding proteins, syndapin2 and EHBP1. Additionally, the EH domain of EHD2, which facilitates canonical EHD protein interactions, was not required to direct overexpressed EHD2 to the cell surface. On the other hand, several lines of evidence indicate that the plasma membrane phospholipid phosphatidylinositol 4,5-bisphosphate (PIP2) plays a crucial role in regulating EHD2 subcellular localization. Pharmacologic perturbation of PIP2 metabolism altered PIP2 plasma membrane distribution (as assessed by confocal microscopy), and caused EHD2 to redistribute away from the plasma membrane. Furthermore, overexpressed EHD2 localized to PIP2-enriched vacuoles generated by active Arf6. Finally, we show that although cytochalasin D caused actin microfilaments to collapse, EHD2 was nevertheless maintained at the plasma membrane. Intriguingly, cytochalasin D induced relocalization of both PIP2 and EHD2 to actin aggregates, supporting a role of PIP2 in controlling EHD2 subcellular localization. Altogether, these studies emphasize the significance of membrane lipid composition for EHD2 subcellular distribution and offer new insights into the regulation of this important endocytic protein.

Indexed as

Actin CytoskeletonAdaptor Proteins, Signal TransducingADP-Ribosylation Factor 6ADP-Ribosylation FactorsCarrier ProteinsCell MembraneCytochalasin DGene ExpressionHeLa CellsHumansMicroscopy, ConfocalPhosphatidylinositol 4,5-DiphosphateProtein BindingProtein Structure, TertiaryProtein TransportVacuolesAdaptor Proteins, Signal TransducingADP-Ribosylation Factor 6ADP-Ribosylation FactorsARF6 protein, humanCarrier ProteinsCytochalasin DEHBP1 protein, humanEHD2 protein, humanPACSIN2 protein, humanPhosphatidylinositol 4,5-Diphosphate

Identifiers

PMID24040268
PMCPMC3769341
OpenAlexW2015263799

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.