Evidence map›Paper›PMID 24088567›Full record

ArticleMolecular biology of the cell2013

Supervillin binding to myosin II and synergism with anillin are required for cytokinesis.

Tara C Smith, Peter C Fridy, Yinyin Li, Shruti Basil, Sneha Arjun, Ryan M Friesen, John Leszyk, Brian T Chait, Michael P Rout, Elizabeth J Luna

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.6field-weighted citation impact, top 18% 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

22 citing papers in PubMed, 39 citations in OpenAlex.

  1. Review
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    Review
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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

10 authors at 2 institutions in 1 country.

Tara C SmithProgram in Cell and Developmental Dynamics, Department of Cell and Developmental Biology, University of Massachusetts Medical School, Worcester, MA 01655 Laboratory of Cellular and Structural Biology, Rockefeller University, New York, NY 10065 Laboratory of Mass Spectrometry and Gaseous Ion Chemistry, Rockefeller University, New York, NY 10065 Proteomics and Mass Spectrometry Facility, University of Massachusetts Medical School, Shrewsbury, MA 01545.
Peter C Fridy
Yinyin Li
Shruti Basil
Sneha Arjun
Ryan M Friesen
John Leszyk
Brian T Chait
Michael P Rout
Elizabeth J Luna
University of Massachusetts Chan Medical School · USRockefeller University · US

Funding

National Resource for Mass Spectrom of Biological MacromoleculesP41GM103314 · NIGMS · ROCKEFELLER UNIVERSITY · PI CHAIT, BRIAN T · 2012 to 2017
$9.9M
New Tools for Exploring the Dynamic Interactome (Renewal)U54GM103511 · NIGMS · ROCKEFELLER UNIVERSITY · PI ROUT, MICHAEL P · 2012 to 2013
$6.2M
CYTOSKELTON-MEMBRANE INTERACTIONSR01GM033048 · NIGMS · WORCESTER FOUNDATION FOR BIOMEDICAL RES · PI LUNA, ELIZABETH J. · 1985 to 2009
$3.3M
NIGMS NIH HHS P41 GM103314NIGMS NIH HHS R01 GM033048NIGMS NIH HHS R01 GM033048-26S1NIGMS NIH HHS U54 GM103511
6 · The paper itself

Abstract

Cytokinesis, the process by which cytoplasm is apportioned between dividing daughter cells, requires coordination of myosin II function, membrane trafficking, and central spindle organization. Most known regulators act during late cytokinesis; a few, including the myosin II-binding proteins anillin and supervillin, act earlier. Anillin's role in scaffolding the membrane cortex with the central spindle is well established, but the mechanism of supervillin action is relatively uncharacterized. We show here that two regions within supervillin affect cell division: residues 831-1281, which bind central spindle proteins, and residues 1-170, which bind the myosin II heavy chain (MHC) and the long form of myosin light-chain kinase. MHC binding is required to rescue supervillin deficiency, and mutagenesis of this site creates a dominant-negative phenotype. Supervillin concentrates activated and total myosin II at the furrow, and simultaneous knockdown of supervillin and anillin additively increases cell division failure. Knockdown of either protein causes mislocalization of the other, and endogenous anillin increases upon supervillin knockdown. Proteomic identification of interaction partners recovered using a high-affinity green fluorescent protein nanobody suggests that supervillin and anillin regulate the myosin II and actin cortical cytoskeletons through separate pathways. We conclude that supervillin and anillin play complementary roles during vertebrate cytokinesis.

Indexed as

CytokinesisAmino Acid SequenceBinding SitesContractile ProteinsCytoskeletonGene Knockdown TechniquesGreen Fluorescent ProteinsHeLa CellsHumansMembrane ProteinsMicrofilament ProteinsMutagenesisMyosin-Light-Chain KinaseMyosin Type IIPoint MutationProtein BindinganillinContractile Proteinsenhanced green fluorescent proteinGreen Fluorescent ProteinsMembrane ProteinsMicrofilament ProteinsMyosin-Light-Chain KinaseMyosin Type IISVIL protein, human

Identifiers

PMID24088567
PMCPMC3842989
OpenAlexW2118579239

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.