Ubiquitin-dependent c-Jun degradation in vivo is mediated by the delta domain.

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Item Type:	Article
Title:	Ubiquitin-dependent c-Jun degradation in vivo is mediated by the delta domain.
Creators Name:	Treier, M., Staszewski, L.M. and Bohmann, D.
Abstract:	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.
Keywords:	Amino Acid Sequence, Cultured Cells, DNA Mutational Analysis, Endopeptidases, HeLa Cells, Ligases, Lysine, Molecular Sequence Data, Nucleic Acid Regulatory Sequences, Oncogene Protein P65(Gag-Jun), Post-Translational Protein Processing, Protein Conformation, Proto-Oncogene Proteins C-Jun, Recombinant Proteins, Structure-Activity Relationship, Ubiquitins, Animals, Chickens
Source:	Cell
ISSN:	0092-8674
Publisher:	Cell Press
Volume:	78
Number:	5
Page Range:	787-798
Date:	9 September 1994
Official Publication:	https://doi.org/10.1016/S0092-8674(94)90502-9
PubMed:	View item in PubMed

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