Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1936054 | Biochemical and Biophysical Research Communications | 2007 | 5 Pages |
Abstract
The subunit S5a is a key component for the recruitment of ubiquitinated substrates to the 26S proteasome. When the full-length S5a, the N-terminal half of S5a (S5aN) containing the von Willebrand A (vWA) domain, and the C-terminal half of S5a (S5aC) containing two ubiquitin(Ub)-interacting motifs (UIMs) were ectopically expressed in HEK293 cells, Ub-conjugates accumulated most prominently in S5aC-expressing cells. In addition, S5aC induced A549 lung cancer cell death but not non-cancer BEAS-2B cell death. Similar effects were observed using only S5a-UIMs. Our data therefore suggest that S5a-UIMs can be used as upstream inhibitors of the proteasome pathway.
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Authors
Muthukumar Elangovan, Eun Soo Choi, Bong Geom Jang, Mi Sun Kim, Yung Joon Yoo,