N-Terminal and C-Terminal Domains of Calmodulin Mediate FADD and TRADD Interaction |
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| Authors: | Giuliana Papoff Nadia Trivieri Sonia Marsilio Roberta Crielesi Cristiana Lalli Loriana Castellani Edward M Balog Giovina Ruberti |
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| Institution: | 1National Research Council, Institute of Cell Biology and Neurobiology, Campus Adriano Buzzati-Traverso, Monterotondo, Rome, Italy;2Department of Human Sciences, Society and Health, University of Cassino, Cassino, Italy;3School of Applied Physiology, Georgia Institute of Technology, Atlanta, Georgia, United States of America;University of Alabama at Birmingham, UNITED STATES |
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| Abstract: | FADD (Fas–associated death domain) and TRADD (Tumor Necrosis Factor Receptor 1-associated death domain) proteins are important regulators of cell fate in mammalian cells. They are both involved in death receptors mediated signaling pathways and have been linked to the Toll-like receptor family and innate immunity. Here we identify and characterize by database search analysis, mutagenesis and calmodulin (CaM) pull-down assays a calcium-dependent CaM binding site in the α-helices 1–2 of TRADD death domain. We also show that oxidation of CaM methionines drastically reduces CaM affinity for FADD and TRADD suggesting that oxidation might regulate CaM-FADD and CaM-TRADD interactions. Finally, using Met-to-Leu CaM mutants and binding assays we show that both the N- and C-terminal domains of CaM are important for binding. |
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