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First published online 5 January 2006
doi: 10.1242/dev.02201

Development 133, 559-568 (2006)
Published by The Company of Biologists 2006
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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

Jana Voigt and Nancy Papalopulu*

The Wellcome Trust/Cancer Research UK Gurdon Institute, Tennis Court Road, Cambridge, CB2 1QR, UK and Department of Anatomy, Downing Site, University of Cambridge, Cambridge, CB2 3DY, UK.

* Author for correspondence (e-mail: np209{at}mole.bio.cam.ac.uk)

Accepted 7 November 2005

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 ß-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 ß-catenin and an increase in total ß-catenin. Our results show that Cullin-1-mediated protein degradation plays an essential role in the correct allocation of neural crest fates during embryogenesis.

Key words: Cullin-1, SCF, Neural crest, ß-catenin, Ubiquitin, Protein degradation, Xenopus






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