Abstract
Background: Calmodulin (CaM) is recruited into the death-inducing signaling complex in cholangiocarcinoma cells. Results: CaM binds to FasDD in a 2:1 CaM:FasDD model. CaM antagonists abolish FasDD-CaM interactions. Conclusion: Data offer a structural basis for Fas-CaM interactions and mechanisms of inhibition. Significance: Elucidating the structural determinants of Fas-CaM interaction is critical to understanding the functional role of CaM in Fas-mediated apoptosis.
Original language | English (US) |
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Pages (from-to) | 21898-21908 |
Number of pages | 11 |
Journal | Journal of Biological Chemistry |
Volume | 288 |
Issue number | 30 |
DOIs | |
State | Published - Jul 26 2013 |
Externally published | Yes |
ASJC Scopus subject areas
- Biochemistry
- Molecular Biology
- Cell Biology