Evidence map›Paper›PMID 26864625›Full record

ArticleMolecular biology of the cell2016

Confined diffusion of transmembrane proteins and lipids induced by the same actin meshwork lining the plasma membrane.

Takahiro K Fujiwara, Kokoro Iwasawa, Ziya Kalay, Taka A Tsunoyama, Yusuke Watanabe, Yasuhiro M Umemura, Hideji Murakoshi, Kenichi G N Suzuki, Yuri L Nemoto, Nobuhiro Morone and 1 more

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 96 papers.

0numbers the graph read from it
0cells of the map it votes in
96citing papers in PubMed
12.4field-weighted citation impact, top 1% 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

96 citing papers in PubMed, 208 citations in OpenAlex.

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  13. Lipid Membrane Domains Control Actin Network Viscoelasticity.Langmuir : the ACS journal of surfaces and colloids · 2024
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36 more citing papers are in PubMed but not listed here.

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

11 authors at 6 institutions in 3 countries.

Takahiro K FujiwaraCenter for Meso-Bio Single-Molecule Imaging, Institute for Integrated Cell-Material Sciences, Kyoto 606-8501, Japan.
Kokoro IwasawaInstitute for Frontier Medical Sciences, Kyoto University, Kyoto 606-8507, Japan.
Ziya KalayInstitute for Integrated Cell-Material Sciences, Kyoto 606-8507, Japan.
Taka A TsunoyamaInstitute for Integrated Cell-Material Sciences, Kyoto 606-8507, Japan.
Yusuke WatanabeInstitute for Integrated Cell-Material Sciences, Kyoto 606-8507, Japan.
Yasuhiro M UmemuraDepartment of Physiology and Systems Bioscience, Kyoto Prefectural University of Medicine, Kyoto 602-8566, Japan.
Hideji MurakoshiNational Institute for Physiological Sciences, Okazaki 444-8585, Japan.
Kenichi G N SuzukiInstitute for Integrated Cell-Material Sciences, Kyoto 606-8507, Japan Institute for Stem Cell Biology and Regenerative Medicine and National Centre for Biological Sciences, Bangalore 650056, India.
Yuri L NemotoInstitute for Integrated Cell-Material Sciences, Kyoto 606-8507, Japan.
Nobuhiro MoroneMRC Toxicology Unit, University of Leicester, Leicester LE1 9HN, United Kingdom.
Akihiro KusumiInstitute for Frontier Medical Sciences, Kyoto University, Kyoto 606-8507, Japan Institute for Integrated Cell-Material Sciences, Kyoto 606-8507, Japan Membrane Cooperativity Unit, Okinawa Institute of Science and Technology, Onna-son, Okinawa 904-0412, Japan akusumi@frontier.kyoto-u.ac.jp.
Kyoto Prefectural University of Medicine · JPKyoto University · JPNational Centre for Biological Sciences · INNational Institute for Physiological Sciences · JPOkinawa Institute of Science and Technology Graduate University · JPUniversity of Leicester · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The mechanisms by which the diffusion rate in the plasma membrane (PM) is regulated remain unresolved, despite their importance in spatially regulating the reaction rates in the PM. Proposed models include entrapment in nanoscale noncontiguous domains found in PtK2 cells, slow diffusion due to crowding, and actin-induced compartmentalization. Here, by applying single-particle tracking at high time resolutions, mainly to the PtK2-cell PM, we found confined diffusion plus hop movements (termed "hop diffusion") for both a nonraft phospholipid and a transmembrane protein, transferrin receptor, and equal compartment sizes for these two molecules in all five of the cell lines used here (actual sizes were cell dependent), even after treatment with actin-modulating drugs. The cross-section size and the cytoplasmic domain size both affected the hop frequency. Electron tomography identified the actin-based membrane skeleton (MSK) located within 8.8 nm from the PM cytoplasmic surface of PtK2 cells and demonstrated that the MSK mesh size was the same as the compartment size for PM molecular diffusion. The extracellular matrix and extracellular domains of membrane proteins were not involved in hop diffusion. These results support a model of anchored TM-protein pickets lining actin-based MSK as a major mechanism for regulating diffusion.

Indexed as

Actin CytoskeletonAnimalsCell LineCell MembraneDiffusionHumansModels, BiologicalPhospholipidsPotoroidaeRatsReceptors, TransferrinPhospholipidsReceptors, Transferrin

Identifiers

PMID26864625
PMCPMC4814218
OpenAlexW2299243614

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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.