Abstract
Major work elucidating the structure and function of the CD95 death inducing signaling complex (DISC) was carried in the late 1990s. Since then the DISC has become a paradigm for multiprotein signaling complexes in the apoptosis literature. We analyzed the earliest events of DISC formation with a set of different techniques and found a surprising new characteristic of the CD95 DISC. Data revealed that CD95 is palmitoylated on cysteine 199. This lipid modification enhances receptor aggregation to the high molecular weight DISC.
Original language | English (US) |
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Title of host publication | Programmed Cell Death,General Principles forStudying Cell Death, Part A |
Editors | Roya Khosravi-Far, Zahra Zakeri, Richard Lockshin, Mauro Piacentini |
Pages | 83-100 |
Number of pages | 18 |
DOIs | |
State | Published - 2008 |
Publication series
Name | Methods in Enzymology |
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Volume | 442 |
ISSN (Print) | 0076-6879 |
Funding
The work was supported by the National Institutes of Health (R01 CA93519).
ASJC Scopus subject areas
- Biochemistry
- Molecular Biology