ArticleScientific reports2016
Characterisation of assembly and ubiquitylation by the RBCC motif of Trim5α.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 29 citations in OpenAlex.
- Study of retroviral restrictions in a Tadarida bat cell line enlightens specific early blocks and TRIM5 locus multiplication.Journal of virology · 2026Article
- Biophysical evolution of the receptor-binding domains of SARS-CoVs.Biophysical journal · 2023Article
- Structural and functional asymmetry of RING trimerization controls priming and extension events in TRIM5α autoubiquitylation.Nature communications · 2022Article
- Mapping the interaction between Trim28 and the KRAB domain at the center of Trim28 silencing of endogenous retroviruses.Protein science : a publication of the Protein Society · 2022Article
- Editing of the TRIM5 Gene Decreases the Permissiveness of Human T Lymphocytic Cells to HIV-1.Viruses · 2020Article
- Restriction of HIV-1 and other retroviruses by TRIM5.Nature reviews. Microbiology · 2019Review
- Article
- Retrovirus Restriction by TRIM5α: RINGside at a Cage Fight.Cell host & microbe · 2018Article
- A helical LC3-interacting region mediates the interaction between the retroviral restriction factor Trim5α and mammalian autophagy-related ATG8 proteins.The Journal of biological chemistry · 2018Article
- RING tetramerization is required for nuclear body biogenesis and PML sumoylation.Nature communications · 2018Article
- Rhesus monkey TRIM5α protein SPRY domain contributes to AP-1 activation.The Journal of biological chemistry · 2018Article
- General Model for Retroviral Capsid Pattern Recognition by TRIM5 Proteins.Journal of virology · 2018Article
- TRIM5α SPRY/coiled-coil interactions optimize avid retroviral capsid recognition.PLoS pathogens · 2017Article
- Solution NMR structure of the TRIM21 B-box2 and identification of residues involved in its interaction with the RING domain.PloS one · 2017Article
- Closing the net on retroviruses.eLife · 2016Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The post-entry restriction factor Trim5α blocks infection of retroviral pathogens shortly after the virus gains entry to the cell, preventing reverse transcription and integration into the host genome. Central to the mechanism of restriction is recognition of the lattice of capsid protein that forms the inner-shell of the retrovirus. To recognise this lattice, Trim5α has been shown to assemble into a large hexagonal array, complementary to the capsid lattice. Structures of the Trim5α coiled-coil region reveal an elongated anti-parallel dimer consistent with the edges of this array placing the Bbox domain at each end of the coiled-coil to facilitate assembly. To investigate the nature of this assembly we have designed and characterised a monomeric version of the TRIM RBCC motif with a truncated coiled-coil. Biophysical characterisation by SEC-MALLS, AUC, and SAXS demonstrate that this construct forms compact folded domain that assembles into a trimer that would support the formation of a hexagonal lattice. Furthermore, the RING domain and elements of the coiled-coil region are shown to contribute to assembly. Ubiquitylation assays demonstrate that this assembly increases ubiquitylation activity providing a link from recognition of the capsid lattice and assembly to the activation of innate immune signalling and restriction.
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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.