TRPM7 N-terminal region forms complexes with calcium binding proteins CaM and S100A1

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F21%3A00549345" target="_blank" >RIV/61388963:_____/21:00549345 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/00216208:11320/21:10434931 RIV/00216208:11130/21:10434931

Výsledek na webu

<a href="https://doi.org/10.1016/j.heliyon.2021.e08490" target="_blank" >https://doi.org/10.1016/j.heliyon.2021.e08490</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.heliyon.2021.e08490" target="_blank" >10.1016/j.heliyon.2021.e08490</a>

Jazyk výsledku

angličtina

Název v původním jazyce

TRPM7 N-terminal region forms complexes with calcium binding proteins CaM and S100A1

Popis výsledku v původním jazyce

Transient receptor potential melastatin 7 (TRPM7) represents melastatin TRP channel with two significant functions, cation permeability and kinase activity. TRPM7 is widely expressed among tissues and is therefore involved in a variety of cellular functions representing mainly Mg2+ homeostasis, cellular Ca2+ flickering, and the regulation of DNA transcription by a cleaved kinase domain translocated to the nucleus. TRPM7 participates in several important biological processes in the nervous and cardiovascular systems. Together with the necessary function of the TRPM7 in these tissues and its recently analyzed overall structure, this channel requires further studies leading to the development of potential therapeutic targets. Here we present the first study investigating the N-termini of TRPM7 with binding regions for important intracellular modulators calmodulin (CaM) and calcium-binding protein S1 (S100A1) using in vitro and in silico approaches. Molecular simulations of the discovered complexes reveal their potential binding interfaces with common interaction patterns and the important role of basic residues present in the N-terminal binding region of TRPM.

Název v anglickém jazyce

TRPM7 N-terminal region forms complexes with calcium binding proteins CaM and S100A1

Popis výsledku anglicky

Transient receptor potential melastatin 7 (TRPM7) represents melastatin TRP channel with two significant functions, cation permeability and kinase activity. TRPM7 is widely expressed among tissues and is therefore involved in a variety of cellular functions representing mainly Mg2+ homeostasis, cellular Ca2+ flickering, and the regulation of DNA transcription by a cleaved kinase domain translocated to the nucleus. TRPM7 participates in several important biological processes in the nervous and cardiovascular systems. Together with the necessary function of the TRPM7 in these tissues and its recently analyzed overall structure, this channel requires further studies leading to the development of potential therapeutic targets. Here we present the first study investigating the N-termini of TRPM7 with binding regions for important intracellular modulators calmodulin (CaM) and calcium-binding protein S1 (S100A1) using in vitro and in silico approaches. Molecular simulations of the discovered complexes reveal their potential binding interfaces with common interaction patterns and the important role of basic residues present in the N-terminal binding region of TRPM.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10608 - Biochemistry and molecular biology

Projekt

<a href="/cs/project/GA19-04099S" target="_blank" >GA19-04099S: Role interakční sítě nukleofosminu v akutní myeloidní leukémii s mutovaným NPM</a><br>

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2021

Kód důvěrnosti údajů

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

Název periodika

Heliyon

ISSN

2405-8440

e-ISSN

2405-8440

Svazek periodika

7

Číslo periodika v rámci svazku

12

Stát vydavatele periodika

GB - Spojené království Velké Británie a Severního Irska

Počet stran výsledku

7

Strana od-do

e08490

Kód UT WoS článku

000748925400017

EID výsledku v databázi Scopus

2-s2.0-85120421898