Characterization of the part of N-terminal PIP2 binding site of the TRPM1 channel

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11310%2F15%3A10315319" target="_blank" >RIV/00216208:11310/15:10315319 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/67985823:_____/15:00454381 RIV/61388971:_____/15:00454381 RIV/61388963:_____/15:00454381 RIV/00216208:11120/15:43910370 a 2 dalších

Výsledek na webu

<a href="http://dx.doi.org/10.1016/j.bpc.2015.10.005" target="_blank" >http://dx.doi.org/10.1016/j.bpc.2015.10.005</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.bpc.2015.10.005" target="_blank" >10.1016/j.bpc.2015.10.005</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Characterization of the part of N-terminal PIP2 binding site of the TRPM1 channel

Popis výsledku v původním jazyce

Transient receptor potential melastatin-1 (TRPM1) is a calcium channel that is essential for the depolarization of photo-responsive retinal bipolar cells, but most of the physiological functions and cellular roles of this channel are still poorly understood. Most transient receptor potential (TRP) channels are typically regulated by intracellular proteins and other-signaling molecules. Phosphatidylinositol-4,5 bisphosphate (PIP2), a minor phospholipid component of cell membranes, has previously been shown to directly bind TRP channels and to play a unique role in modulating receptor function. To characterize the binding of PIP2 as a potential regulator of TRPM1, we utilized biophysical methods and molecular modeling to study the interactions of PIP2 with an N-terminal fragment of TRPM1 (residues A451-N566). The basic N-terminal residue 1(464 of TRPM1 suggests that it is part of putative pleckstrin homology (PH) domain and is involved in the interactions with PIP2. This is the first report detailing the binding of PIP2 at the N-terminus of the TRPM1 receptor.

Název v anglickém jazyce

Characterization of the part of N-terminal PIP2 binding site of the TRPM1 channel

Popis výsledku anglicky

Transient receptor potential melastatin-1 (TRPM1) is a calcium channel that is essential for the depolarization of photo-responsive retinal bipolar cells, but most of the physiological functions and cellular roles of this channel are still poorly understood. Most transient receptor potential (TRP) channels are typically regulated by intracellular proteins and other-signaling molecules. Phosphatidylinositol-4,5 bisphosphate (PIP2), a minor phospholipid component of cell membranes, has previously been shown to directly bind TRP channels and to play a unique role in modulating receptor function. To characterize the binding of PIP2 as a potential regulator of TRPM1, we utilized biophysical methods and molecular modeling to study the interactions of PIP2 with an N-terminal fragment of TRPM1 (residues A451-N566). The basic N-terminal residue 1(464 of TRPM1 suggests that it is part of putative pleckstrin homology (PH) domain and is involved in the interactions with PIP2. This is the first report detailing the binding of PIP2 at the N-terminus of the TRPM1 receptor.

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

CE - Biochemie

OECD FORD obor

—

Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

S - Specificky vyzkum na vysokych skolach<br>I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2015

Kód důvěrnosti údajů

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

Název periodika

Biophysical Chemistry

ISSN

0301-4622

e-ISSN

—

Svazek periodika

207

Číslo periodika v rámci svazku

December

Stát vydavatele periodika

NL - Nizozemsko

Počet stran výsledku

8

Strana od-do

135-142

Kód UT WoS článku

000366442800016

EID výsledku v databázi Scopus

2-s2.0-84946236868