Evidence map›Paper›PMID 22419816›Full record

ArticleMolecular biology of the cell2012

Myosin-X functions in polarized epithelial cells.

Katy C Liu, Damon T Jacobs, Brian D Dunn, Alan S Fanning, Richard E Cheney

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
1.5field-weighted citation impact, top 19% 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

27 citing papers in PubMed, 41 citations in OpenAlex.

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  15. Myosin MyTH4-FERM structures highlight important principles of convergent evolution.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  16. Article
  17. Article
  18. Article
  19. Myosin-X and disease.Experimental cell research · 2015
    Review
  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

5 authors at 1 institution in 1 country.

Katy C LiuDepartment of Cell and Molecular Physiology, School of Medicine, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, USA.
Damon T Jacobs
Brian D Dunn
Alan S Fanning
Richard E Cheney
University of North Carolina at Chapel Hill · US

Funding

The Platelet-Leukocyte Switch in Vascular DiseaseP01HL080166 · NHLBI · UNIV OF NORTH CAROLINA CHAPEL HILL · PI JACOBSON, KENNETH A · 2006 to 2010
$6.7M
Myosin-X: A Novel Myosin with PH DomainsR01DC003299 · NIDCD · UNIV OF NORTH CAROLINA CHAPEL HILL · PI CHENEY, RICHARD E · 2002 to 2017
$4.4M
ZO-1 & Cytoplasmic Scaffolding of the Tight JunctionR01DK061397 · NIDDK · UNIV OF NORTH CAROLINA CHAPEL HILL · PI FANNING, ALAN SCOTT · 2003 to 2012
$3.4M
ZO-1 & Cytoplasmic Scaffolding of the Tight JunctionR56DK061397 · NIDDK · UNIV OF NORTH CAROLINA CHAPEL HILL · PI ANDERSON, JAMES M. · 2008 to 2008
$327k
MYOSIN-X A NOVEL MYOSIN WITH PH DOMAINSR29DC003299 · NIDCD · UNIVERSITY OF NORTH CAROLINA CHAPEL HILL · PI CHENEY, RICHARD E · 1997 to 2001
$202k
Function of Myosin-X in Intestinal Apical Domain AssemblyF30DK089695 · NIDDK · UNIV OF NORTH CAROLINA CHAPEL HILL · PI LIU, KATY C · 2010 to 2013
$93k
NHLBI NIH HHS HL080166NHLBI NIH HHS P01 HL080166NIDCD NIH HHS DC03299NIDCD NIH HHS R01 DC003299NIDCD NIH HHS R29 DC003299NIDDK NIH HHS 1F30DK089695-01NIDDK NIH HHS DK061397NIDDK NIH HHS F30 DK089695NIDDK NIH HHS R01 DK061397NIDDK NIH HHS R56 DK061397
6 · The paper itself

Abstract

Myosin-X (Myo10) is an unconventional myosin that localizes to the tips of filopodia and has critical functions in filopodia. Although Myo10 has been studied primarily in nonpolarized, fibroblast-like cells, Myo10 is expressed in vivo in many epithelia-rich tissues, such as kidney. In this study, we investigate the localization and functions of Myo10 in polarized epithelial cells, using Madin-Darby canine kidney II cells as a model system. Calcium-switch experiments demonstrate that, during junction assembly, green fluorescent protein-Myo10 localizes to lateral membrane cell-cell contacts and to filopodia-like structures imaged by total internal reflection fluorescence on the basal surface. Knockdown of Myo10 leads to delayed recruitment of E-cadherin and ZO-1 to junctions, as well as a delay in tight junction barrier formation, as indicated by a delay in the development of peak transepithelial electrical resistance (TER). Although Myo10 knockdown cells eventually mature into monolayers with normal TER, these monolayers do exhibit increased paracellular permeability to fluorescent dextrans. Importantly, knockdown of Myo10 leads to mitotic spindle misorientation, and in three-dimensional culture, Myo10 knockdown cysts exhibit defects in lumen formation. Together these results reveal that Myo10 functions in polarized epithelial cells in junction formation, regulation of paracellular permeability, and epithelial morphogenesis.

Indexed as

AnimalsCadherinsCell LineCell Membrane PermeabilityCell PolarityDogsEpithelial CellsGene Knockdown TechniquesKidneyMyosinsPseudopodiaTight JunctionsZonula Occludens-1 ProteinCadherinsMyosinsZonula Occludens-1 Protein

Identifiers

PMID22419816
PMCPMC3338435
OpenAlexW2026788959

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.