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Calclium-Calmodulin Regulation Of Trpm2 Currents, Brian M. W. Lockhart
Calclium-Calmodulin Regulation Of Trpm2 Currents, Brian M. W. Lockhart
Electronic Thesis and Dissertation Repository
TRPM2 (1507 amino acids), a non-selective cation channel with substantial permeability for Ca2+, is responsive to oxidative stress, and is a mediator of cell death in several cell types. Ca2+-calmodulin has been shown to promote channel activation and inactivation, however the mechanisms are not fully understood. Identifying candidate CaM binding sites using in silico screening, I hypothesized that Ca2+-dependent inactivation (CDI) of TRPM2 is mediated by an intracellular CaM binding domain unique from that of activation (406-415AA). I systematically determined the minimum binding domains for three CaM candidate sites on TRPM2’s intracellular domains using …