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Open AccessJournal ArticleDOI

PIP2 is a necessary cofactor for ion channel function: how and why?

Byung-Chang Suh, +1 more
- 07 May 2008 - 
- Vol. 37, Iss: 1, pp 175-195
TLDR
This review discusses the dependence of ion channels on phosphoinositides and considers possible mechanisms by which PIP2 and analogues regulate ion channel activity.
Abstract
Phosphatidylinositol 4,5-bisphosphate (PIP2) is a minority phospholipid of the inner leaflet of plasma membranes. Many plasma membrane ion channels and ion transporters require PIP2 to function and can be turned off by signaling pathways that deplete PIP2. This review discusses the dependence of ion channels on phosphoinositides and considers possible mechanisms by which PIP2 and analogues regulate ion channel activity.

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Citations
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Journal ArticleDOI

Phosphoinositides: Tiny Lipids With Giant Impact on Cell Regulation

TL;DR: This review is an attempt to give an overview of this enormous research field focusing on major developments in diverse areas of basic science linked to cellular physiology and disease.
Journal ArticleDOI

Hyperpolarization-activated cation channels: from genes to function.

TL;DR: Recent insights into the structure, function, and cellular regulation of HCN channels are summarized and evidence on the role of individual HCN channel types arising from the analysis ofHCN knockout mouse models is discussed.
Journal ArticleDOI

MLKL Compromises Plasma Membrane Integrity by Binding to Phosphatidylinositol Phosphates

TL;DR: It is demonstrated that the full four-helical bundle domain (4HBD) in the N-terminal region of MLKL is required and sufficient to induce its oligomerization and trigger cell death, and found that a patch of positively charged amino acids on the surface of the 4HBD binds to phosphatidylinositol phosphates (PIPs) and allows recruitment ofMLKL to the plasma membrane.
Journal ArticleDOI

hERG K+ Channels: Structure, Function, and Clinical Significance

TL;DR: The human ether-a-go-go related gene (hERG) encodes the pore-forming subunit of the rapid component of the delayed rectifier K(+) channel, Kv11.1, which is the gene product involved in chromosome 7-associated long QT syndrome (LQTS), an inherited disorder associated with a markedly increased risk of ventricular arrhythmias and sudden cardiac death.
Journal ArticleDOI

PI(3,5)P2 controls membrane trafficking by direct activation of mucolipin Ca2+ release channels in the endolysosome

TL;DR: It is proposed that TRPMLs regulate membrane trafficking by transducing information regarding PI(3,5)P(2) levels into changes in juxtaorganellar Ca(2+), thereby triggering membrane fusion/fission events.
References
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Journal ArticleDOI

Phosphoinositides in cell regulation and membrane dynamics

TL;DR: Inositol phospholipids mediate acute responses, but also act as constitutive signals that help define organelle identity, and play a fundamental part in controlling membrane–cytosol interfaces.
Journal ArticleDOI

Identification of a cold receptor reveals a general role for TRP channels in thermosensation

TL;DR: These findings, together with the previous identification of the heat-sensitive channels VR1 and VRL-1, demonstrate that TRP channels detect temperatures over a wide range and are the principal sensors of thermal stimuli in the mammalian peripheral nervous system.
Journal ArticleDOI

Amiloride-sensitive epithelial Na+ channel is made of three homologous subunits.

TL;DR: The ion-selective permeability, the gating properties and the pharmacological profile of the channel formed by coexpressing the three subunits in oocytes are similar to that of the native channel.
Journal ArticleDOI

An Introduction to TRP Channels

TL;DR: The aim of this review is to provide a basic framework for understanding the function of mammalian transient receptor potential (TRP) channels, particularly as they have been elucidated in heterologous expression systems.
Journal ArticleDOI

Bradykinin and nerve growth factor release the capsaicin receptor from PtdIns(4,5)P2-mediated inhibition.

TL;DR: It is shown that bradykinin- or NGF-mediated potentiation of thermal sensitivity in vivo requires expression of VR1, a heat-activated ion channel on sensory neurons, and biochemical studies suggest that VR1 associates with this complex.
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