Interaction between TRP channels and anoctamins.

Cell Calcium

Division of Cell Signaling, National Institute for Physiological Sciences, National Institutes of Natural Sciences, 5-1 Aza-Higashiyama, Myodaiji, Okazaki, Aichi, Japan; Thermal Biology Group, Exploratory Research Center on Life and Living Systems, National Institutes of Natural Sciences, 5-1 Aza-Higashiyama, Myodaiji, Okazaki, Aichi, Japan; Thermal Biology Research Group, Nagoya Advanced Research and Development Center, Nagoya City University, Kawasumi 1, Mizuho-cho, Mizuho-ku, Nagoya, Aichi, Japan. Electronic address:

Published: July 2024

AI Article Synopsis

  • * TRP channels are crucial non-selective cation channels involved in various physiological functions across different body tissues, with significant research beginning after the discovery of TRPV1 in 1997.
  • * The review focuses on recent insights into how ANO1 interacts with specific TRP channels (like TRPV4, TRPC6, TRPV3, TRPV1, and TRPC2) in multiple tissues, indicating that ANO1 may regulate functions via chloride ion movement in those areas.

Article Abstract

Anoctamin 1 (ANO1) binds to transient receptor potential (TRP) channels (protein-protein interaction) and then is activated by TRP channels (functional interaction). TRP channels are non-selective cation channels that are expressed throughout the body and play roles in multiple physiological functions. Studies on TRP channels increased after the identification of TRP vanilloid 1 (TRPV1) in 1997. Calcium-activated chloride channel anoctamin 1 (ANO1, also called TMEM16A and DOG1) was identified in 2008. ANO1 plays a major role in TRP channel-mediated functions, as first shown in 2014 with the demonstration of a protein-protein interaction between TRPV4 and ANO1. In cells that co-express TRP channels and ANO1, calcium entering cells through activated TRP channels causes ANO1 activation. Therefore, in many tissues, the physiological functions related to TRP channels are modulated through chloride flux associated with ANO1 activation. In this review, we summarize the latest understanding of TRP-ANO1 interactions, particularly interaction of ANO1 with TRPV4, TRP canonical 6 (TRPC6), TRPV3, TRPV1, and TRPC2 in the salivary glands, blood vessels, skin keratinocytes, primary sensory neurons, and vomeronasal organs, respectively.

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Source
http://dx.doi.org/10.1016/j.ceca.2024.102912DOI Listing

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