NDLI: Phosphoinositide-mediated gating of inwardly rectifying K+ channels

Content Provider	Springer Nature Link
Author	Logothetis, Diomedes E. Jin, Taihao Lupyan, Dmitry Rosenhouse Dantsker, Avia
Copyright Year	2007
Abstract	Phosphoinositides, such as phosphatidylinositol-bisphosphate (PIP2), control the activity of many ion channels in yet undefined ways. Inwardly, rectifying potassium (Kir) channels were the first shown to be dependent on direct interactions with phosphoinositides. Alterations in channel-PIP2 interactions affect Kir single-channel gating behavior. Aberrations in channel-PIP2 interactions can lead to human disease. As the activity of all Kir channels depends on their interactions with phosphoinositides, future research will aim to understand the molecular events that occur from phosphoinositide binding to channel gating. The determination of atomic resolution structures for several mammalian and bacterial Kir channels provides great promise towards this goal. We have mapped onto the three-dimensional channel structure the position of basic residues identified through mutagenesis studies that contribute to the sensitivity of a Kir channel to PIP2. The localization of these putative PIP2-interacting residues relative to the channel’s permeation pathway has given rise to a testable model, which could account for channel activation by PIP2.
Starting Page	83
Ending Page	95
Page Count	13
File Format	PDF
ISSN	00316768
Journal	Pflügers Archiv
Volume Number	455
Issue Number	1
e-ISSN	14322013
Language	English
Publisher	Springer-Verlag
Publisher Date	2007-05-23
Publisher Place	Berlin, Heidelberg
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Channel-PIP2 interactions Inward rectifiers Ion channels Human Physiology
Content Type	Text
Resource Type	Article
Subject	Physiology Physiology (medical) Clinical Biochemistry

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