Evidence map›Paper›PMID 31877064›Full record

ArticleMolecular biology of the cell2020

Synergistic factors control kinase-phosphatase organization in B-cells engaged with supported bilayers.

Marcos Francisco Núñez, Kathleen Wisser, Sarah L Veatch

Open access · bronzeAbstract read
In one paragraph

Article in Molecular biology of the cell, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
1.0field-weighted citation impact, top 23% 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

8 citing papers in PubMed, 15 citations in OpenAlex.

  1. Review
  2. The plasma membrane as an adaptable fluid mosaic.Biochimica et biophysica acta. Biomembranes · 2023
    Review
  3. Article
  4. Article
  5. Lipid-based and protein-based interactions synergize transmembrane signaling stimulated by antigen clustering of IgE receptors.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  6. Article
  7. Critical Phenomena in Plasma Membrane Organization and Function.Annual review of physical chemistry · 2021
    Review
  8. Review
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

3 authors at 1 institution in 1 country.

Marcos Francisco NúñezDepartment of Biophysics, University of Michigan, Ann Arbor, MI 48105.
Kathleen WisserDepartment of Biophysics, University of Michigan, Ann Arbor, MI 48105.
Sarah L VeatchDepartment of Biophysics, University of Michigan, Ann Arbor, MI 48105.
University of Michigan · US

Funding

Ion channel regulation by heterogeneous membranesR01GM110052 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI VEATCH, SARAH L · 2014 to 2022
$2.9M
NIGMS NIH HHS R01 GM110052
6 · The paper itself

Abstract

B-cells become activated by ligands with varying valency and mode of presentation to the B-cell receptor (BCR). We previously demonstrated that clustering the immunoglobulin M (IgM) isotype of BCR with an artificial soluble cross-linker stabilized an ordered phase-like domain that enriched kinases and depleted phosphatases to promote receptor tyrosine phosphorylation. BCR is also activated by ligands presented at surfaces, and here we activate B-cells via supported bilayers of phosphatidylcholine lipids, a natural ligand for the IgM BCR expressed in the CH27 cells used. Using superresolution fluorescence localization microscopy, along with a quantitative cross-correlation analysis, we find that BRCs engaged with bilayers sort minimal peptide markers of liquid-ordered and liquid-disordered phases, indicating that ordered-domain stabilization is a general feature of BCR clustering. The phosphatase CD45 is more strongly excluded from bilayer-engaged BRCs than a transmembrane peptide, indicating that mechanisms other than domain partitioning contribute to its organization. Experimental observations are assembled into a minimal model of receptor activation that incorporates both ordered domains and direct phosphatase exclusion mechanisms to produce a more sensitive response.

Indexed as

AnimalsBiomarkersB-LymphocytesCell LineComputer SimulationImmunoglobulin MLeukocyte Common AntigensLigandsLipid BilayersMembrane MicrodomainsMicePeptidesPhosphatidylcholinesPhosphorylationPhosphotyrosineProtein-Tyrosine KinasesBiomarkersImmunoglobulin MLeukocyte Common AntigensLigandsLipid BilayersPeptidesPhosphatidylcholinesPhosphotyrosineProtein-Tyrosine KinasesProtein Tyrosine PhosphatasesReceptors, Antigen, B-Cell

Identifiers

PMID31877064
PMCPMC7202075
OpenAlexW2997304618

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.