Journal
JOURNAL OF GENERAL PHYSIOLOGY
Volume 152, Issue 6, Pages -Publisher
ROCKEFELLER UNIV PRESS
DOI: 10.1085/jgp.201912499
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Funding
- Consejo Nacional de Ciencia y Tecnologia [252644]
- Direccion General de Asuntos del Personal Academico, Universidad Nacional Autonoma de Mexico, Programa de Apoyo a Proyectos de Investigacion e Innovacion Tecnologica [IN209515]
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Slow inactivation has been described in multiple voltage-gated K+ channels and in great detail in the Drosophila Shaker channel. Structural studies have begun to facilitate a better understanding of the atomic details of this and other gating mechanisms. To date, the only voltage-gated potassium channels whose structure has been solved are KvAP (x-ray diffraction), the K(V)1.2-K(V)2.1 paddle chimera (x-ray diffraction and cryo-EM), K(V)1.2 (x-ray diffraction), and ether-a-go-go (cryo-EM); however, the structural details and mechanisms of slow inactivation in these channels are unknown or poorly characterized. Here, we present a detailed study of slow inactivation in the rat K(V)1.2 channel and show that it has some properties consistent with the C-type inactivation described in Shaker. We also study the effects of some mutations that are known to modulate C-type inactivation in Shaker and show that qualitative and quantitative differences exist in their functional effects, possibly underscoring subtle but important structural differences between the C-inactivated states in Shaker and K(V)1.2.
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