The ubiquitin-interacting motif of 26S proteasome subunit S5a induces A549 lung cancer cell death
| Autor: | Mi Sun Kim, Yung Joon Yoo, Muthukumar Elangovan, Bong Geom Jang, Eun Soo Choi |
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| Rok vydání: | 2007 |
| Předmět: |
Programmed cell death
Proteasome Endopeptidase Complex biology Ubiquitin-interacting motif Cell Death Ubiquitin Protein subunit HEK 293 cells Biophysics RNA-Binding Proteins Cell Biology Biochemistry Molecular biology Ubiquitin ligase Cell Line Protein Structure Tertiary Lung cancer cell Proteasome biology.protein Humans Cloning Molecular Molecular Biology |
| Zdroj: | Biochemical and biophysical research communications. 364(2) |
| ISSN: | 1090-2104 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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