Evidence map›Paper›PMID 33154161›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2020

Correlated cryogenic fluorescence microscopy and electron cryo-tomography shows that exogenous TRIM5α can form hexagonal lattices or autophagy aggregates in vivo.

Stephen D Carter, João I Mamede, Thomas J Hope, Grant J Jensen

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
2.7field-weighted citation impact, top 9% 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

19 citing papers in PubMed, 34 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Review
  7. Review
  8. Review
  9. Review
  10. In situ snapshots along a mammalian selective autophagy pathway.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  11. Review
  12. Article
  13. Review
  14. Article
  15. Structure of mitotic chromosomes.Molecular cell · 2021
    Article
  16. Article
  17. Review
  18. Article
  19. 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

4 authors at 2 institutions in 1 country.

Stephen D CarterDivision of Biology and Biological Engineering, California Institute of Technology, Pasadena, CA 91125.ORCID 0000-0002-4237-4276
João I MamedeDepartment of Cell and Developmental Biology, Northwestern University, Chicago, IL 60611.ORCID 0000-0002-6048-1876
Thomas J HopeDepartment of Cell and Developmental Biology, Northwestern University, Chicago, IL 60611.ORCID 0000-0001-7183-8319
Grant J JensenDivision of Biology and Biological Engineering, California Institute of Technology, Pasadena, CA 91125; jensen@caltech.edu.ORCID 0000-0003-1556-4864
California Institute of Technology · USNorthwestern University · US

Funding

Virus TransmissionP50AI150464 · NIAID · UNIVERSITY OF UTAH · PI ECKERT, DEBRA MUIR · 2019 to 2021
$14.9M
Direct live-cell visualization and quantification of interactions between infectious HIV particles in primary target cells.K22AI140963 · NIAID · RUSH UNIVERSITY MEDICAL CENTER · PI INACIO MAMEDE, JOAO FILIPE · 2020 to 2021
$270k
NIAID NIH HHS K22 AI140963NIAID NIH HHS P50 AI150464
6 · The paper itself

Abstract

Members of the tripartite motif (TRIM) protein family have been shown to assemble into structures in both the nucleus and cytoplasm. One TRIM protein family member, TRIM5α, has been shown to form cytoplasmic bodies involved in restricting retroviruses such as HIV-1. Here we applied cryogenic correlated light and electron microscopy, combined with electron cryo-tomography, to intact mammalian cells expressing YFP-rhTRIM5α and found the presence of hexagonal nets whose arm lengths were similar to those of the hexagonal nets formed by purified TRIM5α in vitro. We also observed YFP-rhTRIM5α within a diversity of structures with characteristics expected for organelles involved in different stages of macroautophagy, including disorganized protein aggregations (sequestosomes), sequestosomes flanked by flat double-membraned vesicles (sequestosome:phagophore complexes), sequestosomes within double-membraned vesicles (autophagosomes), and sequestosomes within multivesicular autophagic vacuoles (amphisomes or autolysosomes). Vaults were also seen in these structures, consistent with their role in autophagy. Our data 1) support recent reports that TRIM5α can form both well-organized signaling complexes and nonsignaling aggregates, 2) offer images of the macroautophagy pathway in a near-native state, and 3) reveal that vaults arrive early in macroautophagy.

Indexed as

Antiviral Restriction FactorsAutophagosomesAutophagyCell Line, TumorCryoelectron MicroscopyElectron Microscope TomographyElectronsHeLa CellsHumansMicroscopy, FluorescenceProtein AggregatesTripartite Motif ProteinsUbiquitin-Protein LigasesAntiviral Restriction FactorsProtein AggregatesTRIM5 protein, humanTripartite Motif ProteinsUbiquitin-Protein Ligasesautophagycryo-CLEM/ECTendoplasmic reticulumhexagonal netsTRIM5α-body

Identifiers

PMID33154161
PMCPMC7703684
OpenAlexW3097396032

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.