Proximal C-Terminus Serves as a Signaling Hub for TRPA1 Channel Regulation via Its Interacting Molecules and Supramolecular Complexes

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F67985823%3A_____%2F20%3A00524125" target="_blank" >RIV/67985823:_____/20:00524125 - isvavai.cz</a>

Alternative codes found

RIV/00216208:11310/20:10419427 RIV/00216208:11320/20:10419427

Result on the web

<a href="https://www.frontiersin.org/articles/10.3389/fphys.2020.00189/full" target="_blank" >https://www.frontiersin.org/articles/10.3389/fphys.2020.00189/full</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.3389/fphys.2020.00189" target="_blank" >10.3389/fphys.2020.00189</a>

Result language

angličtina

Original language name

Proximal C-Terminus Serves as a Signaling Hub for TRPA1 Channel Regulation via Its Interacting Molecules and Supramolecular Complexes

Original language description

Our understanding of the general principles of the polymodal regulation of transient receptor potential (TRP) ion channels has grown impressively in recent years as a result of intense efforts in protein structure determination by cryo-electron microscopy. In particular, the high-resolution structures of various TRP channels captured in different conformations, a number of them determined in a membrane mimetic environment, have yielded valuable insights into their architecture, gating properties and the sites of their interactions with annular and regulatory lipids. The correct repertoire of these channels is, however, organized by supramolecular complexes that involve the localization of signaling proteins to sites of action, ensuring the specificity and speed of signal transduction events. As such, TRP ankyrin 1 (TRPA1), a major player involved in various pain conditions, localizes into cholesterol-rich sensory membrane microdomains, physically interacts with calmodulin, associates with the scaffolding A-kinase anchoring protein (AKAP) and forms functional complexes with the related TRPV1 channel. This perspective will contextualize the recent biochemical and functional studies with emerging structural data with the aim of enabling a more thorough interpretation of the results, which may ultimately help to understand the roles of TRPA1 under various physiological and pathophysiological pain conditions. We demonstrate that an alteration to the putative lipid-binding site containing a residue polymorphism associated with human asthma affects the cold sensitivity of TRPA1. Moreover, we present evidence that TRPA1 can interact with AKAP to prime the channel for opening. The structural bases underlying these interactions remain unclear and are definitely worth the attention of future studies.

Czech name

—

Czech description

—

Type

J_imp - Article in a specialist periodical, which is included in the Web of Science database

CEP classification

—

OECD FORD branch

30103 - Neurosciences (including psychophysiology)

Project

<a href="/en/project/GA19-03777S" target="_blank" >GA19-03777S: Molecular Basis of Thermosensitive TRP Ion Channel Regulation in Nociceptive Neurons</a><br>

Continuities

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Publication year

2020

Confidentiality

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Name of the periodical

Frontiers in physiology

ISSN

1664-042X

e-ISSN

—

Volume of the periodical

11

Issue of the periodical within the volume

Mar 12

Country of publishing house

CH - SWITZERLAND

Number of pages

10

Pages from-to

189

UT code for WoS article

000525527400001

EID of the result in the Scopus database

2-s2.0-85082690950