title: 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 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.
authors: National Research Council, Institute of Cell Biology and Neurobiology, Campus Adriano Buzzati-Traverso, Monterotondo, Rome, Italy.
authors: Giuliana
authors: G
authors: Papoff
authors: National Research Council, Institute of Cell Biology and Neurobiology, Campus Adriano Buzzati-Traverso, Monterotondo, Rome, Italy.
authors: Nadia
authors: N
authors: Trivieri
authors: National Research Council, Institute of Cell Biology and Neurobiology, Campus Adriano Buzzati-Traverso, Monterotondo, Rome, Italy.
authors: Sonia
authors: S
authors: Marsilio
authors: National Research Council, Institute of Cell Biology and Neurobiology, Campus Adriano Buzzati-Traverso, Monterotondo, Rome, Italy.
authors: Roberta
authors: R
authors: Crielesi
authors: National Research Council, Institute of Cell Biology and Neurobiology, Campus Adriano Buzzati-Traverso, Monterotondo, Rome, Italy.
authors: Cristiana
authors: C
authors: Lalli
authors: National Research Council, Institute of Cell Biology and Neurobiology, Campus Adriano Buzzati-Traverso, Monterotondo, Rome, Italy; Department of Human Sciences, Society and Health, University of Cassino, Cassino, Italy.
authors: Loriana
authors: L
authors: Castellani
authors: School of Applied Physiology, Georgia Institute of Technology, Atlanta, Georgia, United States of America.
authors: Edward M
authors: EM
authors: Balog
authors: National Research Council, Institute of Cell Biology and Neurobiology, Campus Adriano Buzzati-Traverso, Monterotondo, Rome, Italy.
authors: Giovina
authors: G
authors: Ruberti
mesh_terms: D000595:Amino Acid Sequence; D001665:Binding Sites; D002118:Calcium / Q000378:metabolism; D002147:Calmodulin / Q000737:chemistry* / Q000378:metabolism*; D002460:Cell Line; D053200:Fas-Associated Death Domain Protein / Q000378:metabolism*; D006801:Humans; D008715:Methionine / Q000378:metabolism; D051150:Methionine Sulfoxide Reductases / Q000494:pharmacology; D008969:Molecular Sequence Data; D009154:Mutation; D010084:Oxidation-Reduction; D011485:Protein Binding / Q000187:drug effects; D017434:Protein Structure, Tertiary; D053199:TNF Receptor-Associated Death Domain Protein / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*
chemical_list: D002147:Calmodulin; C505533:FADD protein, human; D053200:Fas-Associated Death Domain Protein; D053199:TNF Receptor-Associated Death Domain Protein; D008715:Methionine; D051150:Methionine Sulfoxide Reductases; C027219:methionine sulfoxide reductase; D002118:Calcium
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