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N-terminal and C-terminal domains of calmodulin mediate FADD and TRADD interaction.


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 ?-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.

SUBMITTER: Papoff G 

PROVIDER: S-EPMC4313936 | biostudies-literature | 2015

REPOSITORIES: biostudies-literature

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N-terminal and C-terminal domains of calmodulin mediate FADD and TRADD interaction.

Papoff Giuliana G   Trivieri Nadia N   Marsilio Sonia S   Crielesi Roberta R   Lalli Cristiana C   Castellani Loriana L   Balog Edward M EM   Ruberti Giovina G  

PloS one 20150202 2


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 deat  ...[more]

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