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ORAI1 channel gating and selectivity is differentially altered by natural mutations in the first or third transmembrane domain.
Bulla M, Gyimesi G, Kim JH, Bhardwaj R, Hediger MA, Frieden M, Demaurex N
J Physiol. 2018 Nov 1. doi: 10.1113/JP277079.
PubMed Article

Plasmids from Article

ID Plasmid Purpose
114180ORAI1-YFP V107MORAI1 channel with C-terminal YFP, carrying the mutation V107M in the protein 1st transmembrane domain, responsible for a constitutive activity and associated with tubular aggregate myopathy (TAM).
114181ORAI1-YFP T184MORAI1 channel with C-terminal YFP, carrying the mutation T184M in the protein 3rd transmembrane domain, responsible for the channel overactivity and associated with tubular aggregate myopathy (TAM).
114182ORAI1-YFP L273D-L276DORAI1 channel with C-terminal YFP, carrying the double mutation L273D-L276D in the STIM1 binding domain, leading to a channel gating deficiency.
114183ORAI1-YFP V107M-L273D-L276DORAI1 channel with C-terminal YFP, carrying the constitutively activating mutation V107M from TAM, and the mutations L273D-L276D leading to a deficiency in STIM1-mediated gating.
114184ORAI1-YFP T184M-L273D-L276DORAI1 channel with C-terminal YFP, carrying the activating mutation T184M from TAM, and the mutations L273D-L276D leading to a deficiency in STIM1-mediated gating.

Antibodies from Article