Structural dynamics of Na+ and Ca2+ interactions with full-size mammalian NCX
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388971%3A_____%2F24%3A00585589" target="_blank" >RIV/61388971:_____/24:00585589 - isvavai.cz</a>
Alternative codes found
RIV/00216208:11310/24:10495162
Result on the web
<a href="https://www.nature.com/articles/s42003-024-06159-9" target="_blank" >https://www.nature.com/articles/s42003-024-06159-9</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1038/s42003-024-06159-9" target="_blank" >10.1038/s42003-024-06159-9</a>
Alternative languages
Result language
angličtina
Original language name
Structural dynamics of Na+ and Ca2+ interactions with full-size mammalian NCX
Original language description
Cytosolic Ca2+ and Na+ allosterically regulate Na+/Ca2+ exchanger (NCX) proteins to vary the NCX-mediated Ca2+ entry/exit rates in diverse cell types. To resolve the structure-based dynamic mechanisms underlying the ion-dependent allosteric regulation in mammalian NCXs, we analyze the apo, Ca2+, and Na+-bound species of the brain NCX1.4 variant using hydrogen-deuterium exchange mass spectrometry (HDX-MS) and molecular dynamics (MD) simulations. Ca2+ binding to the cytosolic regulatory domains (CBD1 and CBD2) rigidifies the intracellular regulatory loop (5L6) and promotes its interaction with the membrane domains. Either Na+ or Ca2+ stabilizes the intracellular portions of transmembrane helices TM3, TM4, TM9, TM10, and their connecting loops (3L4 and 9L10), thereby exposing previously unappreciated regulatory sites. Ca2+ or Na+ also rigidifies the palmitoylation domain (TMH2), and neighboring TM1/TM6 bundle, thereby uncovering a structural entity for modulating the ion transport rates. The present analysis provides new structure-dynamic clues underlying the regulatory diversity among tissue-specific NCX variants.
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
<a href="/en/project/EH22_008%2F0004624" target="_blank" >EH22_008/0004624: PHOTOMACHINES - Photosynthetic cell redesign for high yields of therapeutic peptides</a><br>
Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2024
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Communications Biology
ISSN
2399-3642
e-ISSN
2399-3642
Volume of the periodical
7
Issue of the periodical within the volume
1
Country of publishing house
GB - UNITED KINGDOM
Number of pages
14
Pages from-to
463
UT code for WoS article
001204554200005
EID of the result in the Scopus database
2-s2.0-85190578632