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Can calmodulin bind to lipids of the cytosolic leaflet of plasma membranes?

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388955%3A_____%2F24%3A00598610" target="_blank" >RIV/61388955:_____/24:00598610 - isvavai.cz</a>

  • Alternative codes found

    RIV/61388963:_____/24:00598610 RIV/60076658:12310/24:43908812 RIV/00216224:90127/24:00138505

  • Result on the web

    <a href="https://royalsocietypublishing.org/doi/10.1098/rsob.240067" target="_blank" >https://royalsocietypublishing.org/doi/10.1098/rsob.240067</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1098/rsob.240067" target="_blank" >10.1098/rsob.240067</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Can calmodulin bind to lipids of the cytosolic leaflet of plasma membranes?

  • Original language description

    Calmodulin (CaM) is a ubiquitous calcium-sensitive messenger in eukaryotic cells. It was previously shown that CaM possesses an affinity for diverse lipid moieties, including those found on CaM-binding proteins. These facts, together with our observation that CaM accumulates in membrane-rich protrusions of HeLa cells upon increased cytosolic calcium, motivated us to perform a systematic search for unmediated CaM interactions with model lipid membranes mimicking the cytosolic leaflet of plasma membranes. A range of experimental techniques and molecular dynamics simulations prove unambiguously that CaM interacts with lipid bilayers in the presence of calcium ions. The lipids phosphatidylserine (PS) and phosphatidylethanolamine (PE) hold the key to CaM-membrane interactions. Calcium induces an essential conformational rearrangement of CaM, but calcium binding to the headgroup of PS also neutralizes the membrane negative surface charge. More intriguingly, PE plays a dual role-it not only forms hydrogen bonds with CaM, but also destabilizes the lipid bilayer increasing the exposure of hydrophobic acyl chains to the interacting proteins. Our findings suggest that upon increased intracellular calcium concentration, CaM and the cytosolic leaflet of cellular membranes can be functionally connected.

  • 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

    10403 - Physical chemistry

Result continuities

  • Project

    <a href="/en/project/GX19-26854X" target="_blank" >GX19-26854X: Concert of lipids, ions, and proteins in cell membrane dynamics and function</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

    Open Biology

  • ISSN

    2046-2441

  • e-ISSN

    2046-2441

  • Volume of the periodical

    14

  • Issue of the periodical within the volume

    9

  • Country of publishing house

    GB - UNITED KINGDOM

  • Number of pages

    8

  • Pages from-to

    240067

  • UT code for WoS article

    001313871600001

  • EID of the result in the Scopus database

    2-s2.0-85204512599