Evidence map›Paper›PMID 28096472›Full record

ArticleJournal of cell science2017

Myosin VI facilitates connexin 43 gap junction accretion.

Bennett J Waxse, Prabuddha Sengupta, Geoffrey G Hesketh, Jennifer Lippincott-Schwartz, Folma Buss

Open access · hybridAbstract read
In one paragraph

Article in Journal of cell science, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
1.2field-weighted citation impact, top 22% 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

9 citing papers in PubMed, 21 citations in OpenAlex.

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  5. Overview of the Components of Cardiac Metabolism.Drug metabolism and disposition: the biological fate of chemicals · 2019
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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

5 authors at 3 institutions in 3 countries.

Bennett J WaxseCell Biology and Metabolism Program, Eunice Kennedy Shriver National Institute of Child Health and Human Development, Bethesda, Maryland 20892, USA.
Prabuddha SenguptaCell Biology and Metabolism Program, Eunice Kennedy Shriver National Institute of Child Health and Human Development, Bethesda, Maryland 20892, USA.ORCID 0000-0001-7094-6967
Geoffrey G HeskethMount Sinai Hospital, Lunenfeld-Tanenbaum Research Institute, Toronto, Ontario M5G 1X5, Canada.ORCID 0000-0002-5570-7615
Jennifer Lippincott-SchwartzCell Biology and Metabolism Program, Eunice Kennedy Shriver National Institute of Child Health and Human Development, Bethesda, Maryland 20892, USA lippincottschwartzj@janelia.hhmi.org fb207@cam.ac.uk.ORCID 0000-0002-8601-3501
Folma BussCambridge Institute for Medical Research, University of Cambridge, Cambridge CB2 2XY, UK lippincottschwartzj@janelia.hhmi.org fb207@cam.ac.uk.ORCID 0000-0003-4457-3479
Eunice Kennedy Shriver National Institute of Child Health and Human Development · USUniversity of Cambridge · GBMount Sinai Hospital · CA

Funding

Organization and Dynamics of Endomembrane Pathways and OrganellesZIAHD001609 · NICHD · EUNICE KENNEDY SHRIVER NATIONAL INSTITUTE OF CHILD HEALTH & HUMAN DEVELOPMENT · PI BONIFACINO, JUAN · 2009 to 2019
$16.2M
British Heart Foundation PG/15/12/31280Medical Research Council MR/K000888/1Medical Research Council MR/N000048/1Wellcome Trust 093026Wellcome Trust 100140
6 · The paper itself

Abstract

In this study, we demonstrate myosin VI enrichment at Cx43 (also known as GJA1)-containing gap junctions (GJs) in heart tissue, primary cardiomyocytes and cell culture models. In primary cardiac tissue and in fibroblasts from the myosin VI-null mouse as well as in tissue culture cells transfected with siRNA against myosin VI, we observe reduced GJ plaque size with a concomitant reduction in intercellular communication, as shown by fluorescence recovery after photobleaching (FRAP) and a new method of selective calcein administration. Analysis of the molecular role of myosin VI in Cx43 trafficking indicates that myosin VI is dispensable for the delivery of Cx43 to the cell surface and connexon movement in the plasma membrane. Furthermore, we cannot corroborate clathrin or Dab2 localization at gap junctions and we do not observe a function for the myosin-VI-Dab2 complex in clathrin-dependent endocytosis of annular gap junctions. Instead, we found that myosin VI was localized at the edge of Cx43 plaques by using total internal reflection fluorescence (TIRF) microscopy and use FRAP to identify a plaque accretion defect as the primary manifestation of myosin VI loss in Cx43 homeostasis. A fuller understanding of this derangement may explain the cardiomyopathy or gliosis associated with the loss of myosin VI.

Indexed as

Amino Acid MotifsAnimalsCell CommunicationCell MembraneCells, CulturedConnexin 43Embryo, MammalianFibroblastsGap JunctionsGolgi ApparatusHeLa CellsHumansMiceModels, BiologicalMyocardiumMyocytes, CardiacConnexin 43Myosin Heavy Chainsmyosin VIConnexinEndocytosisGap junctionMyosin

Identifiers

PMID28096472
PMCPMC5358335
OpenAlexW2578545340

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.