Evidence map›Paper›PMID 28122209›Full record

ReviewBiophysical journal2017

Mechanochemical Signaling Directs Cell-Shape Change.

Eric S Schiffhauer, Douglas N Robinson

Abstract readReview
In one paragraph

Review in Biophysical journal, 2017. 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
–field-weighted citation impact
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.

  1. Article
  2. Review
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  4. Review
  5. Article
  6. Review
  7. Review
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  11. Article
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  13. Review
  14. Meddling with myosin's mechanobiology in cancer.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  15. Article
  16. Article
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  18. Article
  19. Myosin IIA interacts with the spectrin-actin membrane skeleton to control red blood cell membrane curvature and deformability.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  20. 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

2 authors.

Eric S SchiffhauerDepartment of Cell Biology, Johns Hopkins University, Baltimore, Maryland.
Douglas N RobinsonDepartment of Cell Biology, Johns Hopkins University, Baltimore, Maryland; Department of Pharmacology and Molecular Science, Johns Hopkins University, Baltimore, Maryland; Department of Medicine, School of Medicine, Johns Hopkins University, Baltimore, Maryland; Department of Chemical and Biomolecular Engineering, Whiting School of Engineering, Johns Hopkins University, Baltimore, Maryland. Electronic address: dnr@jhmi.edu.

Funding

The Biochemical Basis for the Mechanics of CytokinesisR01GM066817 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI ROBINSON, DOUGLAS N · 2003 to 2025
$7.3M
Force-sensitive macromolecular cytoskeletal assemblyR01GM109863 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI ROBINSON, DOUGLAS N, ROCK, RONALD S · 2014 to 2017
$1.1M
NIGMS NIH HHS R01 GM066817NIGMS NIH HHS R01 GM109863
6 · The paper itself

Abstract

For specialized cell function, as well as active cell behaviors such as division, migration, and tissue development, cells must undergo dynamic changes in shape. To complete these processes, cells integrate chemical and mechanical signals to direct force production. This mechanochemical integration allows for the rapid production and adaptation of leading-edge machinery in migrating cells, the invasion of one cell into another during cell-cell fusion, and the force-feedback loops that ensure robust cytokinesis. A quantitative understanding of cell mechanics coupled with protein dynamics has allowed us to account for furrow ingression during cytokinesis, a model cell-shape-change process. At the core of cell-shape changes is the ability of the cell's machinery to sense mechanical forces and tune the force-generating machinery as needed. Force-sensitive cytoskeletal proteins, including myosin II motors and actin cross-linkers such as α-actinin and filamin, accumulate in response to internally generated and externally imposed mechanical stresses, endowing the cell with the ability to discern and respond to mechanical cues. The physical theory behind how these proteins display mechanosensitive accumulation has allowed us to predict paralog-specific behaviors of different cross-linking proteins and identify a zone of optimal actin-binding affinity that allows for mechanical stress-induced protein accumulation. These molecular mechanisms coupled with the mechanical feedback systems ensure robust shape changes, but if they go awry, they are poised to promote disease states such as cancer cell metastasis and loss of tissue integrity.

Indexed as

Cell ShapeMechanotransduction, CellularAnimals

Identifiers

PMID28122209
PMCPMC5266144

What OpenQuestion holds

Textmetadata
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.