Pyrin N-Terminal Homology Domain- and Caspase Recruitment Domain-Dependent Oligomerization of ASC

ASC was first identified as a caspase recruitment domain (CARD)-containing proapoptotic molecule that forms insoluble aggregates during apoptosis. Here, we report both the pyrin N-terminal homology domain (PYD) and CARD domains are involved in the aggregation of ASC. Preliminary experiments indicate...

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Bibliographic Details
Published in:Biochemical and biophysical research communications 2001-01, Vol.280 (3), p.652-655
Main Authors: Masumoto, Junya, Taniguchi, Shun'ichiro, Sagara, Junji
Format: Article
Language:English
Subjects:
adaptor
aggregation
Animals
ASC
CARD
CARD Signaling Adaptor Proteins
Caspases - metabolism
COS Cells
Cytoskeletal Proteins - chemistry
Cytoskeletal Proteins - genetics
Cytoskeletal Proteins - metabolism
Dimerization
filament formation
Green Fluorescent Proteins
heterophilic interaction
homophilic interaction
Luminescent Proteins - chemistry
Luminescent Proteins - genetics
Luminescent Proteins - metabolism
oligomerization
Protein Structure, Quaternary
Protein Structure, Tertiary
Proteins - chemistry
PYD
Pyrin
Recombinant Fusion Proteins - chemistry
Recombinant Fusion Proteins - genetics
Recombinant Fusion Proteins - metabolism
Transfection
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Summary:ASC was first identified as a caspase recruitment domain (CARD)-containing proapoptotic molecule that forms insoluble aggregates during apoptosis. Here, we report both the pyrin N-terminal homology domain (PYD) and CARD domains are involved in the aggregation of ASC. Preliminary experiments indicated that overexpression of ASC formed filament-like aggregates in COS-7 cells. Expression experiments using green fluorescent protein (GFP) constructs showed that not only the GFP-ASC-CARD but also the GFP-ASC-PYD formed filament-like aggregates in COS-7 cells. We confirmed these filament-like aggregates of both the ASC-PYD and the ASC-CARD due to homophilic interaction by immunoprecipitation method. We also demonstrated that the ASC-PYD associated with the ASC-CARD by heterophilic interaction. These observations suggest that the dimerization of the PYD as well as the CARD plays an important role in the oligomerization of ASC as an adaptor molecule.
ISSN:0006-291X
1090-2104
DOI:10.1006/bbrc.2000.4190