Evidence map›Paper›PMID 26877082›Full record

ArticleCurrent biology : CB2016

ER-PM Contacts Define Actomyosin Kinetics for Proper Contractile Ring Assembly.

Dan Zhang, Tamara C Bidone, Dimitrios Vavylonis

Abstract read
In one paragraph

Article in Current biology : CB, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed, 1 pooled it
–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

14 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Stay in touch with the endoplasmic reticulum.Science China. Life sciences · 2024
    Pooled it
  2. The ER-PM interaction is essential for cytokinesis and recruits the actin cytoskeleton through the SCAR/WAVE complex.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  3. Article
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  6. Review
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  10. Multiscale model of integrin adhesion assembly.PLoS computational biology · 2019
    Article
  11. Distinct segregation patterns of yeast cell-peripheral proteins uncovered by a method for protein segregatome analysis.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  12. Article
  13. A lipid regulator working at the cleavage furrow.Cell cycle (Georgetown, Tex.) · 2016
    Article
  14. 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

3 authors.

Dan ZhangTemasek Life Sciences Laboratory, 1 Research Link, Singapore 117604, Singapore. Electronic address: zhangdan@tll.org.sg.
Tamara C BidoneDepartment of Physics, Lehigh University, Bethlehem, PA 18015, USA.
Dimitrios VavylonisDepartment of Physics, Lehigh University, Bethlehem, PA 18015, USA. Electronic address: vavylonis@lehigh.edu.

Funding

Modeling and analysis of actin filament organization in yeastR01GM098430 · NIGMS · LEHIGH UNIVERSITY · PI VAVYLONIS, DIMITRIOS · 2012 to 2016
$1.3M
NIGMS NIH HHS R01 GM098430NIGMS NIH HHS R01GM098430
6 · The paper itself

Abstract

The cortical endoplasmic reticulum (ER), an elaborate network of tubules and cisternae [1], establishes contact sites with the plasma membrane (PM) through tethering machinery involving a set of conserved integral ER proteins [2]. The physiological consequences of forming ER-PM contacts are not fully understood. Here, we reveal a kinetic restriction role of ER-PM contacts over ring compaction process for proper actomyosin ring assembly in Schizosaccharomyces pombe. We show that fission yeast cells deficient in ER-PM contacts exhibit aberrant equatorial clustering of actin cables during ring assembly and are particularly susceptible to compromised actin filament crosslinking activity. Using quantitative image analyses and computer simulation, we demonstrate that ER-PM contacts function to modulate the distribution of ring components and to constrain their compaction kinetics. We propose that ER-PM contacts have evolved as important physical modulators to ensure robust ring assembly.

Indexed as

CytokinesisActomyosinCell MembraneEndoplasmic ReticulumKineticsSchizosaccharomycesSchizosaccharomyces pombe ProteinsActomyosinSchizosaccharomyces pombe Proteins

Identifiers

PMID26877082
PMCPMC4783277

What OpenQuestion holds

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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.