Evidence map›Paper›PMID 38036511›Full record

ArticleNature communications2023

A dynamic partitioning mechanism polarizes membrane protein distribution.

Tatsat Banerjee, Satomi Matsuoka, Debojyoti Biswas, Yuchuan Miao, Dhiman Sankar Pal, Yoichiro Kamimura, Masahiro Ueda, Peter N Devreotes, Pablo A Iglesias

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2023. 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
4.3field-weighted citation impact, top 5% 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, 28 citations in OpenAlex.

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  9. Signaling and actin waves at a glance.Journal of cell science · 2025
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  18. Review
  19. Article
  20. [Integrin and N-cadherin Co-Regulate the Polarity of Mesenchymal Stem Cells via Mechanobiological Mechanisms].Sichuan da xue xue bao. Yi xue ban = Journal of Sichuan University. Medical science edition · 2024
    Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

9 authors at 2 institutions in 2 countries.

Tatsat BanerjeeDepartment of Cell Biology and Center for Cell Dynamics, School of Medicine, Johns Hopkins University, Baltimore, MD, USA. tatsatb@jhu.edu.ORCID 0000-0002-3490-3959
Satomi MatsuokaLaboratory for Cell Signaling Dynamics, RIKEN Center for Biosystems Dynamics Research, Suita, Osaka, Japan.ORCID 0000-0002-4552-4460
Debojyoti BiswasDepartment of Electrical and Computer Engineering, Whiting School of Engineering, Johns Hopkins University, Baltimore, MD, USA.ORCID 0000-0003-4141-4034
Yuchuan MiaoDepartment of Cell Biology and Center for Cell Dynamics, School of Medicine, Johns Hopkins University, Baltimore, MD, USA.ORCID 0000-0003-0600-6609
Dhiman Sankar PalDepartment of Cell Biology and Center for Cell Dynamics, School of Medicine, Johns Hopkins University, Baltimore, MD, USA.ORCID 0000-0002-8442-3507
Yoichiro KamimuraLaboratory for Cell Signaling Dynamics, RIKEN Center for Biosystems Dynamics Research, Suita, Osaka, Japan.
Masahiro UedaLaboratory for Cell Signaling Dynamics, RIKEN Center for Biosystems Dynamics Research, Suita, Osaka, Japan.ORCID 0000-0002-9354-3404
Peter N DevreotesDepartment of Cell Biology and Center for Cell Dynamics, School of Medicine, Johns Hopkins University, Baltimore, MD, USA. pnd@jhmi.edu.ORCID 0000-0002-3260-1455
Pablo A IglesiasDepartment of Cell Biology and Center for Cell Dynamics, School of Medicine, Johns Hopkins University, Baltimore, MD, USA. pi@jhu.edu.ORCID 0000-0002-0840-155X
Johns Hopkins University · USRIKEN Center for Biosystems Dynamics Research · JP

Funding

Excitable Networks in Directed Cell MigrationR35GM118177 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI Peter N Devreotes · 2016 to 2026
$12.1M
Zeiss LSM780 Confocal Microscope for a Core FacilityS10OD016374 · OD · JOHNS HOPKINS UNIVERSITY · PI KUO, SCOT CHARLES · 2013 to 2013
$584k
NIGMS NIH HHS R35 GM118177NIH HHS S10 OD016374ODCDC CDC HHS S10 OD016374
6 · The paper itself

Abstract

The plasma membrane is widely regarded as the hub of the numerous signal transduction activities. Yet, the fundamental biophysical mechanisms that spatiotemporally compartmentalize different classes of membrane proteins remain unclear. Using multimodal live-cell imaging, here we first show that several lipid-anchored membrane proteins are consistently depleted from the membrane regions where the Ras/PI3K/Akt/F-actin network is activated. The dynamic polarization of these proteins does not depend upon the F-actin-based cytoskeletal structures, recurring shuttling between membrane and cytosol, or directed vesicular trafficking. Photoconversion microscopy and single-molecule measurements demonstrate that these lipid-anchored molecules have substantially dissimilar diffusion profiles in different regions of the membrane which enable their selective segregation. When these diffusion coefficients are incorporated into an excitable network-based stochastic reaction-diffusion model, simulations reveal that the altered affinity mediated selective partitioning is sufficient to drive familiar propagating wave patterns. Furthermore, normally uniform integral and lipid-anchored membrane proteins partition successfully when membrane domain-specific peptides are optogenetically recruited to them. We propose "dynamic partitioning" as a new mechanism that can account for large-scale compartmentalization of a wide array of lipid-anchored and integral membrane proteins during various physiological processes where membrane polarizes.

Indexed as

ActinsMembrane ProteinsCell MembraneLipid-Linked ProteinsLipidsMembrane MicrodomainsPhosphatidylinositol 3-KinasesActinsLipid-Linked ProteinsLipidsMembrane ProteinsPhosphatidylinositol 3-Kinases

Identifiers

PMID38036511
PMCPMC10689845
OpenAlexW4389160748

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.