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XB-ART-876
Development 2006 Feb 01;1333:559-68. doi: 10.1242/dev.02201.
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A dominant-negative form of the E3 ubiquitin ligase Cullin-1 disrupts the correct allocation of cell fate in the neural crest lineage.

Voigt J , Papalopulu N .


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.

PubMed ID: 16396913
Article link: Development
Grant support: [+]

Species referenced: Xenopus laevis
Genes referenced: cul1 snai2 sox10 sox3 sox9 zic3
GO keywords: neural crest cell development

Disease Ontology terms: DiGeorge syndrome
OMIMs: DIGEORGE SYNDROME; DGS

Article Images: [+] show captions