Evidence map›Paper›PMID 29887500›Full record

ArticleStructure (London, England : 1993)2018

Interactions of the EphA2 Kinase Domain with PIPs in Membranes: Implications for Receptor Function.

Matthieu Chavent, Dimple Karia, Antreas C Kalli, Jan Domański, Anna L Duncan, George Hedger, Phillip J Stansfeld, Elena Seiradake, E Yvonne Jones, Mark S P Sansom

Open access · hybridAbstract read
In one paragraph

Article in Structure (London, England : 1993), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
2.8field-weighted citation impact, top 9% 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

26 citing papers in PubMed, 44 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Article
  6. Eph receptor signaling complexes in the plasma membrane.Trends in biochemical sciences · 2024
    Review
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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

10 authors at 4 institutions in 2 countries.

Matthieu ChaventDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK; Institut de Pharmacologie et de Biologie Structurale IPBS, Université de Toulouse, CNRS, UPS, Toulouse, France.
Dimple KariaDivision of Structural Biology, Wellcome Centre for Human Genetics, University of Oxford, Roosevelt Drive, Oxford OX3 7BN, UK.
Antreas C KalliLeeds Institute of Cancer and Pathology, St James's University Hospital, University of Leeds, Leeds, UK.
Jan DomańskiDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK.
Anna L DuncanDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK.
George HedgerDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK.
Phillip J StansfeldDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK.
Elena SeiradakeDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK.
E Yvonne JonesDivision of Structural Biology, Wellcome Centre for Human Genetics, University of Oxford, Roosevelt Drive, Oxford OX3 7BN, UK.
Mark S P SansomDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK. Electronic address: mark.sansom@bioch.ox.ac.uk.
University of Oxford · GBCentre for Human Genetics · GBInstitut de Pharmacologie et de Biologie Structurale · FRUniversity of Leeds · GB

Funding

Biotechnology and Biological Sciences Research Council BB/I019855/1Biotechnology and Biological Sciences Research Council BB/L002558/1Biotechnology and Biological Sciences Research Council BB/R00126X/1Cancer Research UK 17721Cancer Research UK A17721Medical Research Council MR/L018039/1Wellcome Trust 202827/Z/16/Z
6 · The paper itself

Abstract

EphA2 is a member of the receptor tyrosine kinase family. Interactions of the cytoplasmic region of EphA2 with the cell membrane are functionally important and yet remain incompletely characterized. Molecular dynamics simulations combined with biochemical studies reveal the interactions of the transmembrane, juxtamembrane (JM), and kinase domains with the membrane. We describe how the kinase domain is oriented relative to the membrane and how the JM region can modulate this interaction. We highlight the role of phosphatidylinositol phosphates (PIPs) in mediating the interaction of the kinase domain with the membrane and, conversely, how positively charged patches at the kinase surface and in the JM region induce the formation of nanoclusters of PIP molecules in the membrane. Integration of these results with those from previous studies enable computational reconstitution of a near complete EphA2 receptor within a membrane, suggesting a role for receptor-lipid interactions in modulation of EphA2.

Indexed as

Binding SitesModels, MolecularMolecular Dynamics SimulationPhosphatidylinositol PhosphatesProtein BindingProtein ConformationReceptor, EphA2Phosphatidylinositol PhosphatesReceptor, EphA2cell membraneEphA2 kinasejuxtamembranemolecular dynamicsmulti-scale simulationsphosphatidylinositol phosphates

Identifiers

PMID29887500
PMCPMC6039763
OpenAlexW2806450473

What Socratic 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 Socratic graph.