Počet záznamů: 1
Shared CaM- and S100A1-binding epitopes in the distal TRPM4 N terminus
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SYSNO ASEP 0489614 Druh ASEP J - Článek v odborném periodiku Zařazení RIV J - Článek v odborném periodiku Poddruh J Článek ve WOS Název Shared CaM- and S100A1-binding epitopes in the distal TRPM4 N terminus Tvůrce(i) Boušová, Kristýna (UOCHB-X) ORCID
Heřman, P. (CZ)
Večeř, J. (CZ)
Bednárová, Lucie (UOCHB-X) RID, ORCID
Monincová, Lenka (UOCHB-X)
Majer, Pavel (UOCHB-X)
Vyklický, L. (CZ)
Vondrášek, Jiří (UOCHB-X) RID, ORCID
Teisinger, J. (CZ)Zdroj.dok. FEBS Journal - ISSN 1742-464X
Roč. 285, č. 3 (2018), s. 599-613Poč.str. 15 s. Jazyk dok. eng - angličtina Země vyd. GB - Velká Británie Klíč. slova calmodulin ; fluorescence anisotropy ; ligand-binding domains ; S100A1 ; TRPM4 channel Vědní obor RIV CE - Biochemie Obor OECD Biochemistry and molecular biology Institucionální podpora UOCHB-X - RVO:61388963 UT WOS 000424168600012 EID SCOPUS 85039160201 DOI 10.1111/febs.14362 Anotace 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 calcium-binding 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. Pracoviště Ústav organické chemie a biochemie Kontakt asep@uochb.cas.cz ; Kateřina Šperková, Tel.: 232 002 584 ; Viktorie Chládková, Tel.: 232 002 434 Rok sběru 2019
Počet záznamů: 1