Evidence map›Paper›PMID 26310444›Full record

ArticleMolecular biology of the cell2015

Modeling the roles of protein kinase Cβ and η in single-cell wound repair.

William R Holmes, Laura Liao, William Bement, Leah Edelstein-Keshet

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
0.9field-weighted citation impact, top 26% 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

9 citing papers in PubMed, 19 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. PKCβ1 regulates meiotic cell cycle in mouse oocyte.Cell cycle (Georgetown, Tex.) · 2019
    Article
  7. Cellular mechanisms and signals that coordinate plasma membrane repair.Cellular and molecular life sciences : CMLS · 2018
    Review
  8. Review
  9. Paradoxical signaling regulates structural plasticity in dendritic spines.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
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 4 institutions in 3 countries.

William R HolmesDepartment of Mathematics and Statistics, University of Melbourne, Melbourne, VIC 3010, Australia.
Laura LiaoDepartment of Biomedical Physics, Ryerson University, Toronto, ON M5B 2K3, Canada.
William BementDepartment of Zoology, Laboratory of Cell and Molecular Biology, University of Wisconsin, Madison, WI 53706.
Leah Edelstein-KeshetDepartment of Mathematics, University of British Columbia, Vancouver, BC V6T 1Z2, Canada keshet@math.ubc.ca.
The University of Melbourne · AUToronto Metropolitan University · CAUniversity of British Columbia · CAUniversity of Wisconsin–Madison · US

Funding

Transient cytoskeletal arraysR01GM052932 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI BEMENT, WILLIAM · 1997 to 2023
$7.2M
NIGMS NIH HHS GM52932NIGMS NIH HHS R01 GM052932
6 · The paper itself

Abstract

Wounded cells such as Xenopus oocytes respond to damage by assembly and closure of an array of actin filaments and myosin-2 controlled by Rho GTPases, including Rho and Cdc42. Rho and Cdc42 are patterned around wounds in a characteristic manner, with active Rho concentrating in a ring-like zone inside a larger, ring-like zone of active Cdc42. How this patterning is achieved is unknown, but Rho and Cdc42 at wounds are subject to regulation by other proteins, including the protein kinases C. Specifically, Cdc42 and Rho activity are enhanced by PKCβ and inhibited by PKCη. We adapt a mathematical model of Simon and coworkers to probe the possible roles of these kinases. We show that PKCβ likely affects the magnitude of positive Rho-Abr feedback, whereas PKCη acts on Cdc42 inactivation. The model explains both qualitative and some overall quantitative features of PKC-Rho GTPase regulation. It also accounts for the previous, peculiar observation that ∼ 20% of cells overexpressing PKCη display zone inversions--that is, displacement of active Rho to the outside of the active Cdc42.

Indexed as

Models, BiologicalActin CytoskeletonActinsAnimalsOocytesProtein Kinase CProtein Kinase C betarho GTP-Binding ProteinsSingle-Cell AnalysisWound HealingXenopus laevisActinsProtein Kinase CProtein Kinase C betaprotein kinase Nrho GTP-Binding Proteins

Identifiers

PMID26310444
PMCPMC4710240
OpenAlexW2239802822

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.