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A Ca(v)3.2/Stac1 molecular complex controls T-type channel expression at the plasma membrane

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F16%3A00463982" target="_blank" >RIV/61388963:_____/16:00463982 - isvavai.cz</a>

  • Result on the web

    <a href="http://dx.doi.org/10.1080/19336950.2016.1186318" target="_blank" >http://dx.doi.org/10.1080/19336950.2016.1186318</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1080/19336950.2016.1186318" target="_blank" >10.1080/19336950.2016.1186318</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    A Ca(v)3.2/Stac1 molecular complex controls T-type channel expression at the plasma membrane

  • Original language description

    Low-voltage-activated T-type calcium channels are essential contributors to neuronal physiology where they play complex yet fundamentally important roles in shaping intrinsic excitability of nerve cells and neurotransmission. Aberrant neuronal excitability caused by alteration of T-type channel expression has been linked to a number of neuronal disorders including epilepsy, sleep disturbance, autism, and painful chronic neuropathy. Hence, there is increased interest in identifying the cellular mechanisms and actors that underlie the trafficking of T-type channels in normal and pathological conditions. In the present study, we assessed the ability of Stac adaptor proteins to associate with and modulate surface expression of T-type channels. We report the existence of a Ca(v)3.2/Stac1 molecular complex that relies on the binding of Stac1 to the amino-terminal region of the channel. This interaction potently modulates expression of the channel protein at the cell surface resulting in an increased T-type conductance. Altogether, our data establish Stac1 as an important modulator of T-type channel expression and provide new insights into the molecular mechanisms underlying the trafficking of T-type channels to the plasma membrane.

  • 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

    I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Others

  • Publication year

    2016

  • Confidentiality

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

Data specific for result type

  • Name of the periodical

    Channels

  • ISSN

    1933-6950

  • e-ISSN

  • Volume of the periodical

    10

  • Issue of the periodical within the volume

    5

  • Country of publishing house

    US - UNITED STATES

  • Number of pages

    9

  • Pages from-to

    346-354

  • UT code for WoS article

    000382759700004

  • EID of the result in the Scopus database

    2-s2.0-84969769977