Evidence map›Paper›PMID 28537258›Full record

ArticleNature communications2017

Exploiting the kinesin-1 molecular motor to generate a virus membrane penetration site.

Madhu Sudhan Ravindran, Martin F Engelke, Kristen J Verhey, Billy Tsai

Abstract read
In one paragraph

Article in Nature communications, 2017. 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
–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

27 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. The HSV-1 pUL37 protein promotes cell invasion by regulating the kinesin-1 motor.Proceedings of the National Academy of Sciences of the United States of America · 2024
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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.

Madhu Sudhan RavindranDepartment of Cell and Developmental Biology, University of Michigan Medical School, 109 Zina Pitcher Place, 3043 BSRB, Ann Arbor, Michigan 48109, USA.
Martin F EngelkeDepartment of Cell and Developmental Biology, University of Michigan Medical School, 109 Zina Pitcher Place, 3043 BSRB, Ann Arbor, Michigan 48109, USA.
Kristen J VerheyDepartment of Cell and Developmental Biology, University of Michigan Medical School, 109 Zina Pitcher Place, 3043 BSRB, Ann Arbor, Michigan 48109, USA.ORCID 0000-0001-9329-4981
Billy TsaiDepartment of Cell and Developmental Biology, University of Michigan Medical School, 109 Zina Pitcher Place, 3043 BSRB, Ann Arbor, Michigan 48109, USA.

Funding

Transport of polyomavirus across the ER membraneR01AI064296 · NIAID · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI TSAI, BILLY · 2006 to 2021
$5.5M
Regulation of the molecular motor kinesin-IR01GM070862 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI VERHEY, KRISTEN J. · 2005 to 2018
$4.2M
A novel cytosolic chaperone complex in polyomavirus ER membrane transportR01GM113722 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI TSAI, BILLY · 2015 to 2018
$1.2M
NIAID NIH HHS R01 AI064296NIGMS NIH HHS R01 GM070862NIGMS NIH HHS R01 GM113722
6 · The paper itself

Abstract

Viruses exploit cellular machineries to penetrate a host membrane and cause infection, a process that remains enigmatic for non-enveloped viruses. Here we probe how the non-enveloped polyomavirus SV40 penetrates the endoplasmic reticulum (ER) membrane to reach the cytosol, a crucial infection step. We find that the microtubule-based motor kinesin-1 is recruited to the ER membrane by binding to the transmembrane J-protein B14. Strikingly, this motor facilitates SV40 ER-to-cytosol transport by constructing a penetration site on the ER membrane called a 'focus'. Neither kinesin-2, kinesin-3 nor kinesin-5 promotes foci formation or infection. The specific use of kinesin-1 is due to its unique ability to select posttranslationally modified microtubules for cargo transport and thereby spatially restrict focus formation to the perinucleus. These findings support the idea of a 'tubulin code' for motor-dependent trafficking and establish a distinct kinesin-1 function in which a motor is exploited to create a viral membrane penetration site.

Indexed as

Virus InternalizationAnimalsChlorocebus aethiopsCOS CellsCytosolEndoplasmic ReticulumGene Knockdown TechniquesHEK293 CellsHSP47 Heat-Shock ProteinsHumansIntracellular MembranesIntravital MicroscopyKinesinsMicrotubulesMolecular ChaperonesRNA, Small InterferingDNAJB14 protein, humanHSP47 Heat-Shock ProteinsKinesinsMolecular ChaperonesRNA, Small Interfering

Identifiers

PMID28537258
PMCPMC5458101

What OpenQuestion holds

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LicenceCC BY
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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.