Cell
Volume 78, Issue 5, 9 September 1994, Pages 787-798
Journal home page for Cell

Article
Ubiquitin-dependent c-Jun degradation in vivo is mediated by the δ domain

https://doi.org/10.1016/S0092-8674(94)90502-9Get rights and content

Summary

The role of the ubiquitin-dependent proteolysis system in c-Jun breakdown was investigated. Using in vitro experiments and a novel in vivo assay that utilizes molecularly-tagged ubiquitin and c-Jun proteins, it was shown that c-Jun, but not its transforming counterpart, retroviral v-Jun, can be efficiently multiubiquitinated. Consistently, v-Jun has a longer half-life than c-Jun. Mutagenesis experiments indicate that the reason for the escape of v-Jun from multiubiquitination and its resulting stabilization is the deletion of the δ domain, a stretch of 27 amino acids that is present in c-Jun but not in v-Jun. c-Jun sequences containing the δ domain, when transferred to the bacterial β-galactosidase protein, function as a cis-acting ubiquitination and degradation signal. The correlation between transforming ability and the escape from ubiquitin-dependent degradation described here suggests a novel route to oncogenesis.

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