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

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