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PreprintCited by 1Ubiquitin and proteasome pathwaysProtein Degradation and InhibitorsEnzyme Structure and Function

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‘Identification of RING E3 pseudoligases in the TRIM protein family’

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Dudley-Fraser, Jane, Esposito, Diego, McPhie, Katherine, Morley-Williams, Coltrane, Auchynnikava, Tania, Rittinger, Katrin·2024·bioRxiv (Cold Spring Harbor Laboratory)
DOI 10.1101/2024.10.15.614675

Preprint — published as 10.1038/s41467-025-58807-1

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Abstract

TRIpartite Motif (TRIM) family proteins have diverse roles across a broad variety of cellular functions, which are largely presumed to depend on their ubiquitin E3 ligase activity, conferred by a RING domain. However, recent reports have shown that some TRIMs lack detectable ubiquitination activity in isolation, despite containing a RING domain. Here, we present parallel in cellulo , in vitro , and in silico structure-function analyses of the ubiquitin E3 ligase activity and RING domain structural characteristics of whole TRIM protein family. In-depth follow-up studies of this comprehensive dataset reveals a number of ‘pseudoligases’, whose RING domains have structurally diverged at either the homodimerisation or E2∼ubiquitin interfaces, thereby disrupting their ability to catalyse ubiquitin transfer. Together, these data raise intriguing open questions regarding the unknown TRIM functions in physiology and disease. Graphical Abstract:

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Metadata

Authors
Dudley-Fraser, J., Esposito, D., McPhie, K., Morley-Williams, C., Auchynnikava, T., & Rittinger, K.
Affiliations
The Francis Crick Institute (GB)
Corresponding author
Rittinger, Katrin
ORCID
Venue
bioRxiv (Cold Spring Harbor Laboratory)
Publisher
openRxiv
Published
2024-10-17
DOI
10.1101/2024.10.15.614675
OpenAlex
W4403484491
Cited by
1
References
2
Citations by year
2026: 1
Type
posted content
Language
en
Open access
Licence
www.biorxiv.org/about/FAQ#license (vor)
Locations
  • bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion)
  • RePEc: Research Papers in Economics (submittedVersion)
Funders
  • Francis Crick Institute (CC2075)
  • Cancer Research UK (CC2075)
  • Imperial College London
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Degradation and Inhibitors
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
Keywords
TRIM proteins, RING E3 ubiquitin ligase, homodimerization, structure-function analysis, ubiquitination

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