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Cavβ surface charged residues contribute to the regulation of neuronal calcium channels

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F22%3A00551616" target="_blank" >RIV/61388963:_____/22:00551616 - isvavai.cz</a>

  • Alternative codes found

    RIV/00216208:11110/22:10436258 RIV/00216208:11120/22:43922757

  • Result on the web

    <a href="https://doi.org/10.1186/s13041-021-00887-3" target="_blank" >https://doi.org/10.1186/s13041-021-00887-3</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1186/s13041-021-00887-3" target="_blank" >10.1186/s13041-021-00887-3</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Cavβ surface charged residues contribute to the regulation of neuronal calcium channels

  • Original language description

    Voltage-gated calcium channels are essential regulators of brain function where they support depolarization-induced calcium entry into neurons. They consist of a pore-forming subunit (Cavα1) that requires co-assembly with ancillary subunits to ensure proper functioning of the channel. Among these ancillary subunits, the Cavβ plays an essential role in regulating surface expression and gating of the channels. This regulation requires the direct binding of Cavβ onto Cavα1 and is mediated by the alpha interacting domain (AID) within the Cavα1 subunit and the α binding pocket (ABP) within the Cavβ subunit. However, additional interactions between Cavα1 and Cavβ have been proposed. In this study, we analyzed the importance of Cavβ3 surface charged residues in the regulation of Cav2.1 channels. Using alanine-scanning mutagenesis combined with electrophysiological recordings we identified several amino acids within the Cavβ3 subunit that contribute to the gating of the channel. These findings add to the notion that additional contacts besides the main AID/ABP interaction may occur to fine-tune the expression and properties of the channel.

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database

  • CEP classification

  • OECD FORD branch

    10608 - Biochemistry and molecular biology

Result continuities

  • Project

  • Continuities

    I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Others

  • Publication year

    2022

  • Confidentiality

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

Data specific for result type

  • Name of the periodical

    Molecular Brain

  • ISSN

    1756-6606

  • e-ISSN

    1756-6606

  • Volume of the periodical

    15

  • Issue of the periodical within the volume

    1

  • Country of publishing house

    GB - UNITED KINGDOM

  • Number of pages

    5

  • Pages from-to

    3

  • UT code for WoS article

    000737986100002

  • EID of the result in the Scopus database

    2-s2.0-85122180446