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
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10608 - Biochemistry and molecular biology
Result continuities
Project
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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
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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