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Interhelical interactions within the STIM1 CC1 domain modulate CRAC channel activation

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60076658%3A12310%2F21%3A43904251" target="_blank" >RIV/60076658:12310/21:43904251 - isvavai.cz</a>

  • Result on the web

    <a href="https://www.nature.com/articles/s41589-020-00672-8" target="_blank" >https://www.nature.com/articles/s41589-020-00672-8</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1038/s41589-020-00672-8" target="_blank" >10.1038/s41589-020-00672-8</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Interhelical interactions within the STIM1 CC1 domain modulate CRAC channel activation

  • Original language description

    The calcium release activated calcium channel is activated by the endoplasmic reticulum-resident calcium sensor protein STIM1. On activation, STIM1 C terminus changes from an inactive, tight to an active, extended conformation. A coiled-coil clamp involving the CC1 and CC3 domains is essential in controlling STIM1 activation, with CC1 as the key entity. The nuclear magnetic resonance-derived solution structure of the CC1 domain represents a three-helix bundle stabilized by interhelical contacts, which are absent in the Stormorken disease-related STIM1 R304W mutant. Two interhelical sites between the CC1 alpha(1) and CC1 alpha(2) helices are key in controlling STIM1 activation, affecting the balance between tight and extended conformations. Nuclear magnetic resonance-directed mutations within these interhelical interactions restore the physiological, store-dependent activation behavior of the gain-of-function STIM1 R304W mutant. This study reveals the functional impact of interhelical interactions within the CC1 domain for modifying the CC1-CC3 clamp strength to control the activation of STIM1.

  • 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

    2021

  • Confidentiality

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

Data specific for result type

  • Name of the periodical

    Nature Chemical Biology

  • ISSN

    1552-4450

  • e-ISSN

  • Volume of the periodical

    17

  • Issue of the periodical within the volume

    2

  • Country of publishing house

    US - UNITED STATES

  • Number of pages

    9

  • Pages from-to

    196-204

  • UT code for WoS article

    000583964700004

  • EID of the result in the Scopus database

    2-s2.0-85093962070