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

The result's identifiers

  • Result code in 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>

  • Alternative codes found

    RIV/67985823:_____/15:00454381 RIV/61388971:_____/15:00454381 RIV/61388963:_____/15:00454381 RIV/00216208:11120/15:43910370 and 2 more

  • Result on the web

    <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>

Alternative languages

  • Result language

    angličtina

  • Original language name

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

  • Original language description

    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.

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

  • CEP classification

    CE - Biochemistry

  • OECD FORD branch

Result continuities

  • Project

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

  • Continuities

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

Others

  • Publication year

    2015

  • Confidentiality

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

Data specific for result type

  • Name of the periodical

    Biophysical Chemistry

  • ISSN

    0301-4622

  • e-ISSN

  • Volume of the periodical

    207

  • Issue of the periodical within the volume

    December

  • Country of publishing house

    NL - THE KINGDOM OF THE NETHERLANDS

  • Number of pages

    8

  • Pages from-to

    135-142

  • UT code for WoS article

    000366442800016

  • EID of the result in the Scopus database

    2-s2.0-84946236868