Regular ArticleUbiquitin-Dependent 26S Proteasomal Pathway: A Role in the Degradation of Native Human Liver CYP3A4 Expressed in Saccharomyces Cerevisiae?
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Cited by (39)
Drug Metabolism: Cytochrome P450
2022, Comprehensive PharmacologyLiver cytochrome P450 3A ubiquitination in vivo by gp78/autocrine motility factor receptor and C terminus of Hsp70-interacting protein (CHIP) E3 ubiquitin ligases: Physiological and pharmacological relevance
2010, Journal of Biological ChemistryCitation Excerpt :Accordingly, our studies of heterologous expression of CYP3A4 in wild type Saccharomyces cerevisiae and mutants containing defined genetic lesions in various ERAD components have enabled us to characterize CYP3A ERAD/UPD by identifying several participants such as the ERAD-associated soluble E2 Ub-conjugating enzyme Ubc7p and its membrane anchor Cue1p, Cdc48p-Ufd1p-Npl4 AAA-ATPase complex (homologous to the mammalian p97 complex), and Rpn1p (Hrd2p), an essential 26S proteasomal cap subunit, as important participants in CYP3A ERAD (13, 14, 17). Despite the unambiguous finding that CYP3A4 is indeed degraded in an Ubc7p/Cue1p- and Rpn1p-dependent ERAD process (14, 17), none of the canonical yeast E3 Ub-ligases such as Doa10p or even Hrd1p/Hrd3p involved in the ERAD of several integral and lumenal ER proteins and/or cytosolic proteins (19–27) could be implicated (13, 14, 17). Because this could reflect subtle differences in the recognition of a mammalian CYP3A protein by these yeast Ub-ligases, we examined in vitro CYP3A4 ubiquitination systems functionally reconstituted with purified, recombinant mammalian E2-E3 enzymes.
CYP3A4 ubiquitination by gp78 (the tumor autocrine motility factor receptor, AMFR) and CHIP E3 ligases
2009, Archives of Biochemistry and BiophysicsA role for protein phosphorylation in cytochrome P450 3A4 ubiquitin-dependent proteasomal degradation
2009, Journal of Biological ChemistryCitation Excerpt :Cycloheximide can perturb cellular physiology via translational shut-off of protein synthesis during the relatively longer time courses required to monitor P450 degradation thereby altering this process (58, 59). A regulatable promoter such as GAL1–10 would be ideal, but then in yeast, P450s, including CYP3A4, are very poorly expressed from plasmids under such promoters (4, 5, 60). For these combined reasons, P450 degradation was as described previously (4, 5), monitored by the stationary chase analyses.
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