Evolution, composition and functions of cullin E3 ubiquitin ligases in trypanosomes
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11310%2F25%3A10515721" target="_blank" >RIV/00216208:11310/25:10515721 - isvavai.cz</a>
Result on the web
<a href="https://verso.is.cuni.cz/pub/verso.fpl?fname=obd_publikace_handle&handle=pftHwLBBZO" target="_blank" >https://verso.is.cuni.cz/pub/verso.fpl?fname=obd_publikace_handle&handle=pftHwLBBZO</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1038/s41598-025-32077-9" target="_blank" >10.1038/s41598-025-32077-9</a>
Alternative languages
Result language
angličtina
Original language name
Evolution, composition and functions of cullin E3 ubiquitin ligases in trypanosomes
Original language description
Post-translational modifications (PTMs) modulate protein functions, with ubiquitylation a preeminent example, and playing major roles in protein turnover. Ubiquitylation utilises a ligase enzyme cascade for conjugation of ubiquitin to client proteins, of which there are a large number in humans and lesser numbers in unicellular eukaryotes. The Cullin-RING ligases are amongst the most complex ligase subfamily and are present across the eukaryote lineage. We have reconstructed the evolution of cullin-RING E3 ubiquitin ligases across eukaryotes and experimentally determined the composition of six of seven cullin complexes in trypanosomatids. We find considerable diversity within cullins and reconstruct at least four ancestral pan-eukaryotic subfamilies. Furthermore, we identify expansions of cullin client adaptor protein families, novel client adaptors and demonstrate client specificity in trypanosomatids. We also find evidence for increasing complexity within client adaptors, suggesting ongoing expansion of adapter architecture. Finally, we show that turnover of ornithine decarboxylase (TbODC), an important target of the trypanocide eflornithine, is mediated byTbCul-A/CUL-1. These studies highlight lineage-specific aspects of cullin E3 ligases and their contributions towards eukaryotic complexity.
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10600 - Biological sciences
Result continuities
Project
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Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2025
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Scientific Reports
ISSN
2045-2322
e-ISSN
2045-2322
Volume of the periodical
16
Issue of the periodical within the volume
1
Country of publishing house
GB - UNITED KINGDOM
Number of pages
18
Pages from-to
2285
UT code for WoS article
001665489900001
EID of the result in the Scopus database
2-s2.0-105027871819