期刊
JOURNAL OF GENERAL PHYSIOLOGY
卷 119, 期 1, 页码 105-116出版社
ROCKEFELLER UNIV PRESS
DOI: 10.1085/jgp.119.1.105
关键词
ATP; ADP; K(ir)6.2; SUR; gating mechanism
类别
The ATP-sensitive potassium (K-ATP) channel is named after its characteristic inhibition by intracellular ATP. The inhibition is a centerpiece of how the KATP channel sets electrical signaling to the energy state of the cell. In the beta cell of the endocrine pancreas, for example, ATP inhibition results from high blood glucose levels and turns on electrical activity leading to insulin release. The underlying gating mechanism (ATP inhibition gating) includes ATP stabilization of closed states, but the action of ATP on the open state of the channel is disputed. The original models of ATP inhibition gating proposed that ATP directly binds the open state, whereas recent models indicate a prerequisite transition from the open to a closed state before ATP binds and inhibits activity We tested these two classes of models by using kinetic analysis of single-channel currents from the cloned mouse pancreatic K-ATP channel expressed in Xenopus oocytes. In particular, we combined gating models based on fundamental rate law and burst gating kinetic considerations. The results demonstrate open-state ATP dependence as the major mechanism by which ATP speeds exit from the active burst state underlying inhibition of the K-ATP channel by ATP.
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