Evidence map›Paper›PMID 31599693›Full record

ArticleMolecular biology of the cell2019

Phosphorylation of nephrin induces phase separated domains that move through actomyosin contraction.

Soyeon Kim, Joseph M Kalappurakkal, Satyajit Mayor, Michael K Rosen

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
3.0field-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

28 citing papers in PubMed, 42 citations in OpenAlex.

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  17. Phase separation in immune signalling.Nature reviews. Immunology · 2022
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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

4 authors at 1 institution in 2 countries.

Soyeon KimDepartment of Biophysics and Howard Hughes Medical Institute, University of Texas Southwestern Medical Center, Dallas, TX 75390.
Joseph M KalappurakkalThe HHMI/MBL Summer Institute, Marine Biological Laboratory, Woods Hole, MA 02543.
Satyajit MayorThe HHMI/MBL Summer Institute, Marine Biological Laboratory, Woods Hole, MA 02543.
Michael K RosenDepartment of Biophysics and Howard Hughes Medical Institute, University of Texas Southwestern Medical Center, Dallas, TX 75390.
Marine Biological Laboratory · US

Funding

Wellcome Trust
6 · The paper itself

Abstract

The plasma membrane of eukaryotic cells is organized into lipid and protein microdomains, whose assembly mechanisms and functions are incompletely understood. We demonstrate that proteins in the nephrin/Nck/N-WASP actin-regulatory pathway cluster into micron-scale domains at the basal plasma membrane upon triggered phosphorylation of transmembrane protein nephrin. The domains are persistent but readily exchange components with their surroundings, and their formation is dependent on the number of Nck SH3 domains, suggesting they are phase separated polymers assembled through multivalent interactions among the three proteins. The domains form independent of the actin cytoskeleton, but acto-myosin contractility induces their rapid lateral movement. Nephrin phosphorylation induces larger clusters at the cell periphery, which are associated with extensive actin assembly and dense filopodia. Our studies illustrate how multivalent interactions between proteins at the plasma membrane can produce micron-scale organization of signaling molecules, and how the resulting clusters can both respond to and control the actin cytoskeleton.

Indexed as

Actin CytoskeletonActinsActomyosinAdaptor Proteins, Signal TransducingAnimalsCell MembraneHumansMembrane ProteinsOncogene ProteinsPhosphorylationProtein BindingProtein DomainsProtein Interaction Domains and MotifsSignal Transductionsrc Homology DomainsWiskott-Aldrich Syndrome ProteinActinsActomyosinAdaptor Proteins, Signal TransducingMembrane ProteinsNck proteinnephrinOncogene ProteinsWAS protein, humanWiskott-Aldrich Syndrome Protein

Identifiers

PMID31599693
PMCPMC6857567
OpenAlexW2979404777

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.