TY - JOUR
T1 - Voltage-sensing phosphatase reveals temporal regulation of TRPC3/C6/C7 channels by membrane phosphoinositides
AU - Itsuki, Kyohei
AU - Imai, Yuko
AU - Okamura, Yasushi
AU - Abe, Kihachiro
AU - Inoue, Ryuji
AU - Mori, Masayuki X.
N1 - Funding Information:
ject to self-limiting regulation that is This work was supported by Grants-in-aid related to their close association with the for Young Scientist from the Japan Society PtdIns(4,5)P2-PLC-DAG cascade and for the Promotion of Sciences, The Naito is distinct from the self-limiting mecha-Foundation and Central Research Insitute nisms observed in voltage-gated channels. of Fukuoka University (to M.X.M.).
Copyright:
Copyright 2017 Elsevier B.V., All rights reserved.
PY - 2012
Y1 - 2012
N2 - TRPC3/C6/C7 channels, a subgroup of classical/canonical TRP channels, are activated by diacylglycerol produced via activation of phospholipase C (PLC)-coupled receptors. Recognition of the physiological importance of these channels has been steadily growing, but the mechanism by which they are regulated remains largely unknown. We recently used a membrane-resident Danio rerio voltage-sensing phosphatase (DrVSP) to study TRPC3/C6/C7 regulation and found that the channel activity was controlled by PtdIns(4,5) P2-DAG signaling in a self-limiting manner (Imai Y et al. The Journal of Physiology 2012). In this addendum, we present the advantages of using DrVSP as a molecular tool to study PtdIns(4,5)P2 regulation. DrVSP should be readily applicable for studying phosphoinositide metabolism-linked channel regulation as well as lipid dynamics. Furthermore, in comparison to other modes of self-limiting ion channel regulation, the regulation of TRPC3/C6/C7 channels seems highly susceptible to activation signal strength, which could potentially affect both open duration and the time to peak activation and inactivation. Dysfunction of such self-limiting regulation may contribute to the pathology of the cardiovascular system, gastrointestinal tract and brain, as these channels are broadly distributed and affected by numerous neurohormonal agonists.
AB - TRPC3/C6/C7 channels, a subgroup of classical/canonical TRP channels, are activated by diacylglycerol produced via activation of phospholipase C (PLC)-coupled receptors. Recognition of the physiological importance of these channels has been steadily growing, but the mechanism by which they are regulated remains largely unknown. We recently used a membrane-resident Danio rerio voltage-sensing phosphatase (DrVSP) to study TRPC3/C6/C7 regulation and found that the channel activity was controlled by PtdIns(4,5) P2-DAG signaling in a self-limiting manner (Imai Y et al. The Journal of Physiology 2012). In this addendum, we present the advantages of using DrVSP as a molecular tool to study PtdIns(4,5)P2 regulation. DrVSP should be readily applicable for studying phosphoinositide metabolism-linked channel regulation as well as lipid dynamics. Furthermore, in comparison to other modes of self-limiting ion channel regulation, the regulation of TRPC3/C6/C7 channels seems highly susceptible to activation signal strength, which could potentially affect both open duration and the time to peak activation and inactivation. Dysfunction of such self-limiting regulation may contribute to the pathology of the cardiovascular system, gastrointestinal tract and brain, as these channels are broadly distributed and affected by numerous neurohormonal agonists.
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U2 - 10.4161/chan.20883
DO - 10.4161/chan.20883
M3 - Article
C2 - 22760061
AN - SCOPUS:84864412730
SN - 1933-6950
VL - 6
SP - 206
EP - 209
JO - Channels
JF - Channels
IS - 3
ER -