Interaction of Calmodulin with TRPM: An Initiator of Channel Modulation
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F23%3A00576684" target="_blank" >RIV/61388963:_____/23:00576684 - isvavai.cz</a>
Result on the web
<a href="https://doi.org/10.3390/ijms242015162" target="_blank" >https://doi.org/10.3390/ijms242015162</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.3390/ijms242015162" target="_blank" >10.3390/ijms242015162</a>
Alternative languages
Result language
angličtina
Original language name
Interaction of Calmodulin with TRPM: An Initiator of Channel Modulation
Original language description
Transient receptor potential melastatin (TRPM) channels, a subfamily of the TRP superfamily, constitute a diverse group of ion channels involved in mediating crucial cellular processes like calcium homeostasis. These channels exhibit complex regulation, and one of the key regulatory mechanisms involves their interaction with calmodulin (CaM), a cytosol ubiquitous calcium-binding protein. The association between TRPM channels and CaM relies on the presence of specific CaM-binding domains in the channel structure. Upon CaM binding, the channel undergoes direct and/or allosteric structural changes and triggers down- or up-stream signaling pathways. According to current knowledge, ion channel members TRPM2, TRPM3, TRPM4, and TRPM6 are directly modulated by CaM, resulting in their activation or inhibition. This review specifically focuses on the interplay between TRPM channels and CaM and summarizes the current known effects of CaM interactions and modulations on TRPM channels in cellular physiology.
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
2023
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
International Journal of Molecular Sciences
ISSN
1661-6596
e-ISSN
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Volume of the periodical
24
Issue of the periodical within the volume
20
Country of publishing house
CH - SWITZERLAND
Number of pages
21
Pages from-to
15162
UT code for WoS article
001095430100001
EID of the result in the Scopus database
2-s2.0-85175280181