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- W2013076486 abstract "Selective protein degradation is an efficient and rapid way of terminating protein activity. Defects in protein degradation are associated with a number of human diseases, including potentially DiGeorge syndrome, which is characterised by abnormal development of the neural crest lineage during embryogenesis. We describe the identification of Xenopus Cullin-1, an E3 ubiquitin ligase, and show that blocking the function of endogenous Cullin-1 leads to pleiotropic defects in development. Notably, there is an increased allocation of cells to a neural crest fate and within this lineage, an increase in melanocytes at the expense of cranial ganglia neurons. Most of the observed effects can be attributed to stabilisation of beta-catenin, a known target of Cullin-1-mediated degradation from other systems. Indeed, we show that blocking the function of Cullin-1 leads to a decrease in ubiquitinated beta-catenin and an increase in total beta-catenin. Our results show that Cullin-1-mediated protein degradation plays an essential role in the correct allocation of neural crest fates during embryogenesis." @default.
- W2013076486 created "2016-06-24" @default.
- W2013076486 creator A5065106799 @default.
- W2013076486 creator A5086456495 @default.
- W2013076486 date "2006-02-01" @default.
- W2013076486 modified "2023-09-25" @default.
- W2013076486 title "A dominant-negative form of the E3 ubiquitin ligase<i>Cullin-1</i>disrupts the correct allocation of cell fate in the neural crest lineage" @default.
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- W2013076486 doi "https://doi.org/10.1242/dev.02201" @default.
- W2013076486 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/16396913" @default.
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