Shared CaM- and S100A1-binding epitopes in the distal TRPM4 N terminus

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11320%2F18%3A10371913" target="_blank" >RIV/00216208:11320/18:10371913 - isvavai.cz</a>

Alternative codes found

RIV/67985823:_____/18:00490288 RIV/61388963:_____/18:00489614

Result on the web

<a href="http://dx.doi.org/10.1111/febs.14362" target="_blank" >http://dx.doi.org/10.1111/febs.14362</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1111/febs.14362" target="_blank" >10.1111/febs.14362</a>

Result language

angličtina

Original language name

Shared CaM- and S100A1-binding epitopes in the distal TRPM4 N terminus

Original language description

The transient receptor potential channel of melastatin 4 (TRPM4) belongs to a group of large ion receptors that are involved in countless cell signalling cascades. This unique member is ubiquitously expressed in many human tissues, especially in cardiomyocytes, where it plays an important role in cardiovascular processes. Transient receptor potential channels (TRPs) are usually constituted by intracellular N- and C- termini, which serve as mediators affecting allosteric modulation of channels, resulting in the regulation of the channel function. The TRPs tails contain a number of conserved epitopes that specifically bind the intracellular modulators. Here, we identify new binding sites for the calmodulin (CaM) and S100 calciumbinding protein A1 (S100A1), located in the very distal part of the TRPM4 N terminus. We have used chemically synthesized peptides of the TRPM4, mimicking the binding epitopes, along with fluorescence methods to determine and specify CaM- and S100A1-binding sites. We have found that the ligands binding epitopes at the TRPM4 N terminus overlap, but the interacting mechanism of both complexes is probably different. The molecular models supported by data from the fluorescence method confirmed that the complexes formations are mediated by the positively charged (R139, R140, R144) and hydrophobic (L134, L138, V143) residues present at the TRPM4 N terminus-binding epitopes. The data suggest that the molecular complexes of TRPM4/CaM and TRPM4/S100A1 would lead to the modulation of the channel functions.

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

10608 - Biochemistry and molecular biology

Project

Result was created during the realization of more than one project. More information in the Projects tab.

Continuities

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Publication year

2018

Confidentiality

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

Name of the periodical

FEBS Journal

ISSN

1742-464X

e-ISSN

—

Volume of the periodical

285

Issue of the periodical within the volume

3

Country of publishing house

GB - UNITED KINGDOM

Number of pages

15

Pages from-to

599-613

UT code for WoS article

000424168600012

EID of the result in the Scopus database

2-s2.0-85039160201