Evidence map›Paper›PMID 32259203›Full record

ArticleThe Journal of cell biology2020

Golgi-associated BICD adaptors couple ER membrane penetration and disassembly of a viral cargo.

Chelsey C Spriggs, Somayesadat Badieyan, Kristen J Verhey, Michael A Cianfrocco, Billy Tsai

Abstract read
In one paragraph

Article in The Journal of cell biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing 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

12 citing papers in PubMed.

  1. Article
  2. Viral interference of nucleocytoplasmic transport.The Journal of biological chemistry · 2025
    Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Review
  10. Article
  11. Review
  12. Review
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.

Chelsey C SpriggsDepartment of Cell and Developmental Biology, University of Michigan Medical School, Ann Arbor, MI.
Somayesadat BadieyanDepartment of Biological Chemistry and the Life Sciences Institute, University of Michigan, Ann Arbor, MI.
Kristen J VerheyDepartment of Cell and Developmental Biology, University of Michigan Medical School, Ann Arbor, MI.
Michael A CianfroccoDepartment of Biological Chemistry and the Life Sciences Institute, University of Michigan, Ann Arbor, MI.
Billy TsaiDepartment of Cell and Developmental Biology, University of Michigan Medical School, Ann Arbor, MI.

Funding

Molecular Mechanisms of Microbial Pathogenesis Training ProgramT32AI007528 · NIAID · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI CARRUTHERS, VERNON BRUCE · 1998 to 2024
$6.8M
Kinesin Motors and Microtubule-based TraffickingR35GM131744 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI Kristen J. Verhey · 2019 to 2026
$6.3M
Transport of polyomavirus across the ER membraneR01AI064296 · NIAID · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI TSAI, BILLY · 2006 to 2021
$5.5M
Clarifying the role of the cytoplasmic dynein motor complex in polyomavirus nuclear entry.F32GM133099 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI SPRIGGS, CHELSEY CIERRA · 2019 to 2020
$106k
NIAID NIH HHS R01 AI064296NIAID NIH HHS T32 AI007528NIGMS NIH HHS F32 GM133099
6 · The paper itself

Abstract

During entry, viruses must navigate through the host endomembrane system, penetrate cellular membranes, and undergo capsid disassembly to reach an intracellular destination that supports infection. How these events are coordinated is unclear. Here, we reveal an unexpected function of a cellular motor adaptor that coordinates virus membrane penetration and disassembly. Polyomavirus SV40 traffics to the endoplasmic reticulum (ER) and penetrates a virus-induced structure in the ER membrane called "focus" to reach the cytosol, where it disassembles before nuclear entry to promote infection. We now demonstrate that the ER focus is constructed proximal to the Golgi-associated BICD2 and BICDR1 dynein motor adaptors; this juxtaposition enables the adaptors to directly bind to and disassemble SV40 upon arrival to the cytosol. Our findings demonstrate that positioning of the virus membrane penetration site couples two decisive infection events, cytosol arrival and disassembly, and suggest cargo remodeling as a novel function of dynein adaptors.

Indexed as

AnimalsBiological TransportCell LineCell NucleusCytosolEndocytosisEndoplasmic ReticulumGolgi ApparatusHost-Pathogen InteractionsHumansIntracellular MembranesPolyomavirusVirus Internalization

Identifiers

PMID32259203
PMCPMC7199864

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.