Abstract：
:Ubiquitin chains serve as a recognition motif for the proteasome, a multisubunit protease, which degrades its substrates into polypeptides while releasing ubiquitin for reuse. Yeast proteasomes contain two deubiquitinating enzymes, Ubp6 and Rpn11. Rpn11 promotes protein breakdown through its degradation-coupled activity. In contrast, we show here that Ubp6 has the capacity to delay the degradation of ubiquitinated proteins by the proteasome. However, delay of degradation by Ubp6 does not require its catalytic activity, indicating that Ubp6 has both deubiquitinating activity and proteasome-inhibitory activity. Delay of degradation by Ubp6 appears to provide a time window allowing gradual deubiquitination of the substrate by Ubp6. Rpn11 catalyzes en bloc chain removal, and Ubp6 interferes with degradation at or upstream of this step, so that degradation delay by Ubp6 is accompanied by a switch in the mode of ubiquitin chain processing. We propose that Ubp6 regulates both the nature and magnitude of proteasome activity.
journal_name
Celljournal_title
Cellauthors
Hanna J,Hathaway NA,Tone Y,Crosas B,Elsasser S,Kirkpatrick DS,Leggett DS,Gygi SP,King RW,Finley Ddoi
10.1016/j.cell.2006.07.038subject
Has Abstractpub_date
2006-10-06 00:00:00pages
99-111issue
1eissn
0092-8674issn
1097-4172pii
S0092-8674(06)01208-6journal_volume
127pub_type
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