Please use this identifier to cite or link to this item: http://hdl.handle.net/2381/23730
Title: Identification of human P2X1 receptor-interacting proteins reveals a role of the cytoskeleton in receptor regulation.
Authors: Lalo, U
Roberts, JA
Evans, RJ
First Published: 2-Sep-2011
Citation: J BIOL CHEM, 2011, 286 (35), pp. 30591-30599
Abstract: P2X1 receptors are ATP-gated ion channels expressed by smooth muscle and blood cells. Carboxyl-terminally His-FLAG-tagged human P2X1 receptors were stably expressed in HEK293 cells and co-purified with cytoskeletal proteins including actin. Disruption of the actin cytoskeleton with cytochalasin D inhibited P2X1 receptor currents with no effect on the time course of the response or surface expression of the receptor. Stabilization of the cytoskeleton with jasplakinolide had no effect on P2X1 receptor currents but decreased receptor mobility. P2X2 receptor currents were unaffected by cytochalasin, and P2X1/2 receptor chimeras were used to identify the molecular basis of actin sensitivity. These studies showed that the intracellular amino terminus accounts for the inhibitory effects of cytoskeletal disruption similar to that shown for lipid raft/cholesterol sensitivity. Stabilization of the cytoskeleton with jasplakinolide abolished the inhibitory effects of cholesterol depletion on P2X1 receptor currents, suggesting that lipid rafts may regulate the receptor through stabilization of the cytoskeleton. These studies show that the cytoskeleton plays an important role in P2X1 receptor regulation.
DOI Link: 10.1074/jbc.M111.253153
eISSN: 1083-351X
Links: http://hdl.handle.net/2381/23730
Type: Journal Article
Appears in Collections:Published Articles, Dept. of Cell Physiology and Pharmacology

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