Evidence map›Paper›PMID 28116358›Full record

ArticleScience advances2017

Dynamic interactions between a membrane binding protein and lipids induce fluctuating diffusivity.

Eiji Yamamoto, Takuma Akimoto, Antreas C Kalli, Kenji Yasuoka, Mark S P Sansom

Open access · goldAbstract read
In one paragraph

Article in Science advances, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
3.6field-weighted citation impact, top 6% 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

24 citing papers in PubMed, 78 citations in OpenAlex.

  1. Article
  2. A PI(3,5)PNature communications · 2026
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  10. Review
  11. PIPBiophysical journal · 2021
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  14. 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

5 authors at 3 institutions in 2 countries.

Eiji YamamotoGraduate School of Science and Technology, Keio University, 3-14-1 Hiyoshi, Kohoku-ku, Yokohama 223-8522, Japan.
Takuma AkimotoGraduate School of Science and Technology, Keio University, 3-14-1 Hiyoshi, Kohoku-ku, Yokohama 223-8522, Japan.
Antreas C KalliDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK; Leeds Institute of Cancer and Pathology, School of Medicine, St. James's University Hospital, University of Leeds, Leeds LS9 7TF, UK.
Kenji YasuokaDepartment of Mechanical Engineering, Keio University, 3-14-1 Hiyoshi, Kohoku-ku, Yokohama 223-8522, Japan.
Mark S P SansomDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK.
Keio University · JPSt James's University Hospital · GBUniversity of Oxford · GB

Funding

Wellcome Trust
6 · The paper itself

Abstract

Pleckstrin homology (PH) domains are membrane-binding lipid recognition proteins that interact with phosphatidylinositol phosphate (PIP) molecules in eukaryotic cell membranes. Diffusion of PH domains plays a critical role in biological reactions on membrane surfaces. Although diffusivity can be estimated by long-time measurements, it lacks information on the short-time diffusive nature. We reveal two diffusive properties of a PH domain bound to the surface of a PIP-containing membrane using molecular dynamics simulations. One is fractional Brownian motion, attributed to the motion of the lipids with which the PH domain interacts. The other is temporally fluctuating diffusivity; that is, the short-time diffusivity of the bound protein changes substantially with time. Moreover, the diffusivity for short-time measurements is intrinsically different from that for long-time measurements. This fluctuating diffusivity results from dynamic changes in interactions between the PH domain and PIP molecules. Our results provide evidence that the complexity of protein-lipid interactions plays a crucial role in the diffusion of proteins on biological membrane surfaces. Changes in the diffusivity of PH domains and related membrane-bound proteins may in turn contribute to the formation/dissolution of protein complexes in membranes.

Indexed as

Molecular Dynamics SimulationAdaptor Proteins, Signal TransducingCell MembraneHumansMembrane LipidsMembrane ProteinsProtein DomainsAdaptor Proteins, Signal TransducingDAPP1 protein, humanMembrane LipidsMembrane ProteinsAnomalous diffusionMolecular dynamics simulationsPeripheral membrane proteinsPhosphatidyl-inositol-phosphatePleckstrin homology domains

Identifiers

PMID28116358
PMCPMC5249258
OpenAlexW2574626594

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.