Inhibition of TRPP3 by calmodulin through Ca2+/calmodulin-dependent protein kinase II

Transient receptor potential (TRP) polycystin-3 (TRPP3) is a non-selective cation channel activated by Ca2+ and protons and is involved in regulating ciliary Ca2+ concentration, hedgehog signaling and sour tasting. The TRPP3 channel function and regulation are still not well understood. Here we inve...

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Main Authors: Xiong Liu, Yifang Wang, Ziyi Weng, Qinyi Xu, Cefan Zhou, JingFeng Tang, Xing-Zhen Chen
Format: Article
Language:English
Published: Elsevier 2023-04-01
Series:Cell Insight
Subjects:
Online Access:http://www.sciencedirect.com/science/article/pii/S2772892723000123
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author Xiong Liu
Yifang Wang
Ziyi Weng
Qinyi Xu
Cefan Zhou
JingFeng Tang
Xing-Zhen Chen
author_facet Xiong Liu
Yifang Wang
Ziyi Weng
Qinyi Xu
Cefan Zhou
JingFeng Tang
Xing-Zhen Chen
author_sort Xiong Liu
collection DOAJ
description Transient receptor potential (TRP) polycystin-3 (TRPP3) is a non-selective cation channel activated by Ca2+ and protons and is involved in regulating ciliary Ca2+ concentration, hedgehog signaling and sour tasting. The TRPP3 channel function and regulation are still not well understood. Here we investigated regulation of TRPP3 by calmodulin (CaM) by means of electrophysiology and Xenopus oocytes as an expression model. We found that TRPP3 channel function is enhanced by calmidazolium, a CaM antagonist, and inhibited by CaM through binding of the CaM N-lobe to a TRPP3 C-terminal domain not overlapped with the EF-hand. We further revealed that the TRPP3/CaM interaction promotes phosphorylation of TRPP3 at threonine 591 by Ca2+/CaM-dependent protein kinase II, which mediates the inhibition of TRPP3 by CaM.
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spelling doaj.art-00c587e925fa4d8a9f15d398bb50760b2023-02-19T04:27:47ZengElsevierCell Insight2772-89272023-04-0122100088Inhibition of TRPP3 by calmodulin through Ca2+/calmodulin-dependent protein kinase IIXiong Liu0Yifang Wang1Ziyi Weng2Qinyi Xu3Cefan Zhou4JingFeng Tang5Xing-Zhen Chen6Membrane Protein Disease Research Group, Department of Physiology, Faculty of Medicine and Dentistry, University of Alberta, T6G 2H7, Edmonton, AB, CanadaMembrane Protein Disease Research Group, Department of Physiology, Faculty of Medicine and Dentistry, University of Alberta, T6G 2H7, Edmonton, AB, Canada; National “111'' Center for Cellular Regulation and Molecular Pharmaceutics, Hubei University of Technology, Wuhan, Hubei, 430068, ChinaMembrane Protein Disease Research Group, Department of Physiology, Faculty of Medicine and Dentistry, University of Alberta, T6G 2H7, Edmonton, AB, Canada; National “111'' Center for Cellular Regulation and Molecular Pharmaceutics, Hubei University of Technology, Wuhan, Hubei, 430068, ChinaMembrane Protein Disease Research Group, Department of Physiology, Faculty of Medicine and Dentistry, University of Alberta, T6G 2H7, Edmonton, AB, CanadaNational “111'' Center for Cellular Regulation and Molecular Pharmaceutics, Hubei University of Technology, Wuhan, Hubei, 430068, ChinaNational “111'' Center for Cellular Regulation and Molecular Pharmaceutics, Hubei University of Technology, Wuhan, Hubei, 430068, China; Corresponding author. National ''111'' Center for Cellular Regulation and Molecular Pharmaceutics, Hubei University of Technology, Wuhan, Hubei, 430068, China.Membrane Protein Disease Research Group, Department of Physiology, Faculty of Medicine and Dentistry, University of Alberta, T6G 2H7, Edmonton, AB, Canada; National “111'' Center for Cellular Regulation and Molecular Pharmaceutics, Hubei University of Technology, Wuhan, Hubei, 430068, China; Corresponding author. Membrane Protein Disease Research Group, Department of Physiology, Faculty of Medicine and Dentistry, University of Alberta, T6G 2H7, Edmonton, AB, Canada.Transient receptor potential (TRP) polycystin-3 (TRPP3) is a non-selective cation channel activated by Ca2+ and protons and is involved in regulating ciliary Ca2+ concentration, hedgehog signaling and sour tasting. The TRPP3 channel function and regulation are still not well understood. Here we investigated regulation of TRPP3 by calmodulin (CaM) by means of electrophysiology and Xenopus oocytes as an expression model. We found that TRPP3 channel function is enhanced by calmidazolium, a CaM antagonist, and inhibited by CaM through binding of the CaM N-lobe to a TRPP3 C-terminal domain not overlapped with the EF-hand. We further revealed that the TRPP3/CaM interaction promotes phosphorylation of TRPP3 at threonine 591 by Ca2+/CaM-dependent protein kinase II, which mediates the inhibition of TRPP3 by CaM.http://www.sciencedirect.com/science/article/pii/S2772892723000123TRP channelCaMCalciumCaMK2ElectrophysiologyXenopus oocyte
spellingShingle Xiong Liu
Yifang Wang
Ziyi Weng
Qinyi Xu
Cefan Zhou
JingFeng Tang
Xing-Zhen Chen
Inhibition of TRPP3 by calmodulin through Ca2+/calmodulin-dependent protein kinase II
Cell Insight
TRP channel
CaM
Calcium
CaMK2
Electrophysiology
Xenopus oocyte
title Inhibition of TRPP3 by calmodulin through Ca2+/calmodulin-dependent protein kinase II
title_full Inhibition of TRPP3 by calmodulin through Ca2+/calmodulin-dependent protein kinase II
title_fullStr Inhibition of TRPP3 by calmodulin through Ca2+/calmodulin-dependent protein kinase II
title_full_unstemmed Inhibition of TRPP3 by calmodulin through Ca2+/calmodulin-dependent protein kinase II
title_short Inhibition of TRPP3 by calmodulin through Ca2+/calmodulin-dependent protein kinase II
title_sort inhibition of trpp3 by calmodulin through ca2 calmodulin dependent protein kinase ii
topic TRP channel
CaM
Calcium
CaMK2
Electrophysiology
Xenopus oocyte
url http://www.sciencedirect.com/science/article/pii/S2772892723000123
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