Biochem Biophys Res Commun. 2001 Jan 26;280(3):652-5.

Pyrin N-terminal homology domain- and caspase recruitment domain-dependent oligomerization of ASC.External

Masumoto, J., Taniguchi, S., Sagara, J.,
--- - Department of Molecular Oncology and Angiology, Research Center on Aging and Adaptation, Shinshu University School of Medicine, Asahi 3-1-1, Matsumoto 390-8621, Nagano, Japan.
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.
PMID: 11162571External
Arrow2 In vitro interaction Arrow2 In vivo interaction Arrow2 Characterization Arrow2 Functional role Arrow2 top
In vivo interaction
  Endogenous
expression
Overexpression DD1 DD2 Reference
Family DD1 DD2 Method Species Region Species Region
CARD ASC Link ASC Co-immunoprecipitation COS-7 Not specified 1-100 Not specified 1-100 11162571
PYD ASC Link ASC Co-immunoprecipitation COS-7 Not specified 101-195 Not specified 101-195 11162571
(Link: click this icon to show interactions only between the two corresponding DDs)