Byung-Chang Suh

TL;DR: In this paper, the authors summarize clear evidence supporting the concept that many ion channels are regulated by membrane phosphoinositides, and describe tools used to test their dependence on phosphatidylinositol 4,5-bisphosphate.

TL;DR: In this paper, a family of minority acidic phospholipids in cell membranes, called phosphatidylinositol 4,5-bisphosphate (PIP2), have been shown to contribute to the selection of peripheral proteins for each membrane and regulate the activity of the integral proteins.

TL;DR: Ex vivo endogenous membrane PIP(2) supports high-voltage activated L, N, and P/Q-type Ca(2+) channels, and stimuli that activate phospholipase C deplete PIP (2) and reduce those Ca( 2+) channel currents.

TL;DR: This is a first demonstration of the expression of the P2X7 receptors on neutrophils, which shows that the receptor is functionally involved in the defense mechanism by activation of the respiratory burst pathway.

TL;DR: The model supports the following sequence of events for this Gq-coupled signaling: A classical G-protein cycle, including competition for nucleotide-free G- protein by all nucleotide forms and an activation step requiring Mg2+, followed by G- Protein–stimulated phospholipase C and hydrolysis of PIP2, and finally PIP 2 dissociation from binding sites for inositol lipid on the channels so that KCNQ current was suppressed.