Evidence map›Paper›PMID 27851943›Full record

ArticleBiophysical journal2016

Antagonistic Behaviors of NMY-1 and NMY-2 Maintain Ring Channels in the C. elegans Gonad.

Valerie C Coffman, Torah M Kachur, David B Pilgrim, Adriana T Dawes

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
0.8field-weighted citation impact, top 27% 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

11 citing papers in PubMed, 19 citations in OpenAlex.

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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 2 institutions in 2 countries.

Valerie C CoffmanDepartment of Molecular Genetics, The Ohio State University, Columbus, Ohio.
Torah M KachurDepartment of Biological Sciences, University of Alberta, Edmonton, Alberta Canada.
David B PilgrimDepartment of Biological Sciences, University of Alberta, Edmonton, Alberta Canada.
Adriana T DawesDepartment of Molecular Genetics, The Ohio State University, Columbus, Ohio; Department of Mathematics, The Ohio State University, Columbus, Ohio. Electronic address: dawes.33@osu.edu.
The Ohio State University · USUniversity of Alberta · CA

Funding

Pronuclear rotation in the C. elegans embryoF32GM110977 · NIGMS · OHIO STATE UNIVERSITY · PI COFFMAN, VALERIE CHEST · 2015 to 2017
$109k
NIGMS NIH HHS F32 GM110977
6 · The paper itself

Abstract

Contractile rings play critical roles in a number of biological processes, including oogenesis, wound healing, and cytokinesis. In many cases, the activity of motor proteins such as nonmuscle myosins is required for appropriate constriction of these contractile rings. In the gonad of the nematode worm Caenorhabditis elegans, ring channels are a specialized form of contractile ring that are maintained at a constant diameter before oogenesis. We propose a model of ring channel maintenance that explicitly incorporates force generation by motor proteins that can act normally or tangentially to the ring channel opening. We find that both modes of force generation are needed to maintain the ring channels. We demonstrate experimentally that the type II myosins NMY-1 and NMY-2 antagonize each other in the ring channels by producing force in perpendicular directions: the experimental depletion of NMY-1/theoretical decrease in orthogonal force allows premature ring constriction and cellularization, whereas the experimental depletion of NMY-2/theoretical decrease in tangential force opens the ring channels and prevents cellularization. Together, our experimental and theoretical results show that both forces, mediated by NMY-1 and NMY-2, are crucial for maintaining the appropriate ring channel diameter and dynamics throughout the gonad.

Indexed as

AnimalsCaenorhabditis elegansCaenorhabditis elegans ProteinsGonadsModels, BiologicalMuscle ContractionMyosin Type IIProtein TransportCaenorhabditis elegans ProteinsMyosin Type II

Identifiers

PMID27851943
PMCPMC5113261
OpenAlexW2551899467

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.