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• W2018142757 startingPage "231" @default.
• W2018142757 abstract "KATPchannels are heteromultimers of a sulfonylurea receptor SUR and KIR6.2 with the inward rectifier forming the pore which is regulated by SUR. We have examined the contributions of the cytoplasmic domains of KIR6.2 to control of spontaneous bursting and ATP-inhibition in human SUR1/KIR6.2 KATPchannels. Truncations of the N-terminus of KIR6.2 nearly eliminate transitions to interburst closed states without affecting the open or intraburst closed states, thus producing SUR1/ΔNKIR6.2 channels with an extremely high open probability in the absence of nucleotides. These channels have a decrease apparent ATP-sensitivity which is consistent with the involvement of the N-terminus in a transition to an interburst closed state that preferentially binds inhibitory ATP. Mutations in both the N- and proximal C-termini of KIR6.2 can synergistically attenuate the ATP-inhibition. The results identify the N-terminus of KIR6.2 as a determinant of the interburst kinetics of KATPchannels and suggest that the two cytoplasmic domains of KIR6.2 participate in ATP-inhibitory gating through distinct mechanisms." @default.
• W2018142757 created "2016-06-24" @default.
• W2018142757 creator A5042899461 @default.
• W2018142757 creator A5064513248 @default.
• W2018142757 creator A5086767351 @default.
• W2018142757 date "1999-02-01" @default.
• W2018142757 modified "2023-09-27" @default.
• W2018142757 title "The N-Terminus of KIR6.2 Limits Spontaneous Bursting and Modulates the ATP-Inhibition of KATPChannels" @default.
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• W2018142757 doi "https://doi.org/10.1006/bbrc.1999.0172" @default.
• W2018142757 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/10049691" @default.
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