TRPM6 N-Terminal CaM- and S100A1-Binding Domains

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F19%3A00510200" target="_blank" >RIV/61388963:_____/19:00510200 - isvavai.cz</a>

Alternative codes found

RIV/61388971:_____/19:00510200 RIV/00216208:11320/19:10398900 RIV/00216208:11130/19:10398900

Result on the web

<a href="https://www.mdpi.com/1422-0067/20/18/4430" target="_blank" >https://www.mdpi.com/1422-0067/20/18/4430</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.3390/ijms20184430" target="_blank" >10.3390/ijms20184430</a>

Result language

angličtina

Original language name

TRPM6 N-Terminal CaM- and S100A1-Binding Domains

Original language description

Transient receptor potential (TRPs) channels are crucial downstream targets of calcium signalling cascades. They can be modulated either by calcium itself and/or by calcium-binding proteins (CBPs). Intracellular messengers usually interact with binding domains present at the most variable TRP regions-N- and C-cytoplasmic termini. Calmodulin (CaM) is a calcium-dependent cytosolic protein serving as a modulator of most transmembrane receptors. Although CaM-binding domains are widespread within intracellular parts of TRPs, no such binding domain has been characterised at the TRP melastatin member-the transient receptor potential melastatin 6 (TRPM6) channel. Another CBP, the S100 calcium-binding protein A1 (S100A1), is also known for its modulatory activities towards receptors. S100A1 commonly shares a CaM-binding domain. Here, we present the first identified CaM and S100A1 binding sites at the N-terminal of TRPM6. We have confirmed the L520-R535 N-terminal TRPM6 domain as a shared binding site for CaM and S100A1 using biophysical and molecular modelling methods. A specific domain of basic amino acid residues (R526/R531/K532/R535) present at this TRPM6 domain has been identified as crucial to maintain non-covalent interactions with the ligands. Our data unambiguously confirm that CaM and S100A1 share the same binding domain at the TRPM6 N-terminus although the ligand-binding mechanism is different.

Czech name

—

Czech description

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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

2019

Confidentiality

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

Name of the periodical

International Journal of Molecular Sciences

ISSN

1422-0067

e-ISSN

—

Volume of the periodical

20

Issue of the periodical within the volume

18

Country of publishing house

CH - SWITZERLAND

Number of pages

15

Pages from-to

4430

UT code for WoS article

000489100500109

EID of the result in the Scopus database

2-s2.0-85072047694