期刊
EMBO JOURNAL
卷 26, 期 10, 页码 2454-2464出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/sj.emboj.7601692
关键词
deubiquitination; endosomes; multivesicular bodies; protein sorting
资金
- NIGMS NIH HHS [T32 GM142607, GM08759, R01 GM065505, R01 GM065505-01A1, T32 GM008759] Funding Source: Medline
Doa4 is a ubiquitin-specific protease in Saccharomyces cerevisiae that deubiquitinates integral membrane proteins sorted into the lumenal vesicles of late- endosomal multivesicular bodies (MVBs). We show that the noncatalytic N terminus of Doa4 mediates its recruitment to endosomes through its association with Bro1, which is one of several highly conserved class E Vps proteins that comprise the core MVB sorting machinery. In turn, Bro1 directly stimulates deubiquitination by interacting with a YPxL motif in the catalytic domain of Doa4. Mutations in either Doa4 or Bro1 that disrupt catalytic activation of Doa4 impair deubiquitination and sorting of MVB cargo proteins and lead to the formation of lumenal MVB vesicles that are predominantly small compared with the vesicles seen in wild- type cells. Thus, by recruiting Doa4 to late endosomes and stimulating its catalytic activity, Bro1 fulfills a novel dual role in coordinating deubiquitination in the MVB pathway.
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