Abstract
Ubiquitylation of caspase-8 by the Cullin3 E3 ligase allows its translocation to cytosolic aggregates in the cell by p62/sequesto- some-1, increasing caspase-8 activation and thus leading to TRAIL-induced cell death.
Wong, W Wei-Lynn; Silke, John (2009). Another facet of ubiquitylation: death. Journal of Molecular Cell Biology, 1(2):80-81.
Ubiquitylation of caspase-8 by the Cullin3 E3 ligase allows its translocation to cytosolic aggregates in the cell by p62/sequesto- some-1, increasing caspase-8 activation and thus leading to TRAIL-induced cell death.
Ubiquitylation of caspase-8 by the Cullin3 E3 ligase allows its translocation to cytosolic aggregates in the cell by p62/sequesto- some-1, increasing caspase-8 activation and thus leading to TRAIL-induced cell death.
Item Type: | Journal Article, refereed, further contribution |
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Communities & Collections: | 04 Faculty of Medicine > Institute of Experimental Immunology |
Dewey Decimal Classification: | 570 Life sciences; biology
610 Medicine & health |
Scopus Subject Areas: | Life Sciences > Molecular Biology
Life Sciences > Genetics Life Sciences > Cell Biology |
Language: | English |
Date: | 2009 |
Deposited On: | 15 Jun 2012 15:35 |
Last Modified: | 07 Nov 2023 02:44 |
Publisher: | Oxford University Press |
ISSN: | 1759-4685 |
OA Status: | Closed |
Free access at: | Publisher DOI. An embargo period may apply. |
Publisher DOI: | https://doi.org/10.1093/jmcb/mjp019 |
PubMed ID: | 19797318 |
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