ArticleBMC evolutionary biology2010
Ancient origin of animal U-box ubiquitin ligases.
Article in BMC evolutionary biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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19 citing papers in PubMed, 30 citations in OpenAlex.
- Genome-Wide Identification, Characterization, and Expression Analysis of the U-Box Gene Family in Cucumber (Plants (Basel, Switzerland) · 2025Article
- Genome-Wide Analysis of HECT E3 Ligases Members inInternational journal of molecular sciences · 2024Article
- Deafness-Associated ADGRV1 Mutation Impairs USH2A Stability through Improper Phosphorylation of WHRN and WDSUB1 Recruitment.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2023Article
- Genome-wide analysis of genes encoding core components of the ubiquitin system during cerebral cortex development.Molecular brain · 2022Article
- How Many Faces Does the Plant U-Box E3 Ligase Have?International journal of molecular sciences · 2022Review
- Functional and genomic characterization of patient-derived xenograft model to study the adaptation to mTORC1 inhibitor in clear cell renal cell carcinoma.Cancer medicine · 2021Article
- Identification of potential crucial genes in monocytes for atherosclerosis using bioinformatics analysis.The Journal of international medical research · 2020Article
- Origin and evolution of fungal HECT ubiquitin ligases.Scientific reports · 2018Article
- Specific targeting of the deubiquitinase and E3 ligase families with engineered ubiquitin variants.Bioengineering & translational medicine · 2017Review
- hPso4/hPrp19: a critical component of DNA repair and DNA damage checkpoint complexes.Oncogene · 2016Review
- The eukaryotic ancestor had a complex ubiquitin signaling system of archaeal origin.Molecular biology and evolution · 2015Article
- The role of targeted protein degradation in early neural development.Genesis (New York, N.Y. : 2000) · 2014Review
- The ubiquilin gene family: evolutionary patterns and functional insights.BMC evolutionary biology · 2014Article
- Activity-enhancing mutations in an E3 ubiquitin ligase identified by high-throughput mutagenesis.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Article
- Evolution of plant HECT ubiquitin ligases.PloS one · 2013Article
- HDM2 promotes WIP1-mediated medulloblastoma growth.Neuro-oncology · 2012Article
- Origin and diversification of TRIM ubiquitin ligases.PloS one · 2012Article
- Viral takeover of the host ubiquitin system.Frontiers in microbiology · 2011Article
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1 author at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundThe patterns of emergence and diversification of the families of ubiquitin ligases provide insights about the evolution of the eukaryotic ubiquitination system. U-box ubiquitin ligases (UULs) are proteins characterized by containing a peculiar protein domain known as U box. In this study, the origin of the animal UUL genes is described.
resultsPhylogenetic and structural data indicate that six of the seven main UUL-encoding genes found in humans (UBE4A, UBE4B, UIP5, PRP19, CHIP and CYC4) were already present in the ancestor of all current metazoans and the seventh (WDSUB1) is found in placozoans, cnidarians and bilaterians. The fact that only 4-5 genes orthologous to the human ones are present in the choanoflagellate Monosiga brevicollis suggests that several animal-specific cooptions of the U box to generate new genes occurred. Significantly, Monosiga contains five additional UUL genes that are not present in animals. One of them is also present in distantly-related protozoans. Along animal evolution, losses of UUL-encoding genes are rare, except in nematodes, which lack three of them. These general patterns are highly congruent with those found for other two families (RBR, HECT) of ubiquitin ligases.
conclusionsFinding that the patterns of emergence, diversification and loss of three unrelated families of ubiquitin ligases (RBR, HECT and U-box) are parallel indicates that there are underlying, linage-specific evolutionary forces shaping the complexity of the animal ubiquitin system.
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