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

J 2024

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

SCOLLO, Federica; Carmelo TEMPRA; Hueseyin EVCI; Miguel RIOPEDRE-FERNANDEZ; Agnieszka OLZYNSKA et al.

Základní údaje

Originální název

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

Autoři

Vydání

Open Biology, LONDON, ROYAL SOC, 2024, 2046-2441

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10608 Biochemistry and molecular biology

Stát vydavatele

Velká Británie a Severní Irsko

Utajení

není předmětem státního či obchodního tajemství

Odkazy

URL

Impakt faktor

Impact factor: 3.600

Označené pro přenos do RIV

Ano

Kód RIV

RIV/00216224:90127/24:00138505

Organizační jednotka

CIISB II

Klíčová slova anglicky

calmodulin; lipid membrane; phosphatidylethanolamine; phosphatidylserine; calcium

Štítky

CF NANO, ne MU, rivok

Příznaky

Mezinárodní význam, Recenzováno

Změněno: 16. 1. 2025 15:22, Mgr. Eva Dubská

Anotace

V originále

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.

Návaznosti

90127, velká výzkumná infrastruktura

Název: CIISB II

Citovat

SCOLLO, Federica; Carmelo TEMPRA; Hueseyin EVCI; Miguel RIOPEDRE-FERNANDEZ; Agnieszka OLZYNSKA; Matti JAVANAINEN; Arunima UDAY; Marek CEBECAUER; Lukasz CWIKLIK; Hector MARTINEZ-SEARA; Pavel JUNGWIRTH; Piotr JURKIEWICZ a Martin HOF. Can calmodulin bind to lipids of the cytosolic leaflet of plasma membranes? Open Biology. LONDON: ROYAL SOC, 2024, roč. 14, č. 9, s. 1-8. ISSN 2046-2441. Dostupné z: https://doi.org/10.1098/rsob.240067.

@article{2468552,
   author = {Scollo, Federica and Tempra, Carmelo and Evci, Hueseyin and RiopedreandFernandez, Miguel and Olzynska, Agnieszka and Javanainen, Matti and Uday, Arunima and Cebecauer, Marek and Cwiklik, Lukasz and MartinezandSeara, Hector and Jungwirth, Pavel and Jurkiewicz, Piotr and Hof, Martin},
   article_location = {LONDON},
   article_number = {9},
   doi = {https://doi.org/10.1098/rsob.240067},
   keywords = {calmodulin; lipid membrane; phosphatidylethanolamine; phosphatidylserine; calcium},
   language = {eng},
   issn = {2046-2441},
   journal = {Open Biology},
   title = {Can calmodulin bind to lipids of the cytosolic leaflet of plasma membranes?},
   url = {https://royalsocietypublishing.org/doi/10.1098/rsob.240067},
   volume = {14},
   year = {2024}
}

TY  - JOUR
ID  - 2468552
AU  - Scollo, Federica - Tempra, Carmelo - Evci, Hueseyin - Riopedre-Fernandez, Miguel - Olzynska, Agnieszka - Javanainen, Matti - Uday, Arunima - Cebecauer, Marek - Cwiklik, Lukasz - Martinez-Seara, Hector - Jungwirth, Pavel - Jurkiewicz, Piotr - Hof, Martin
PY  - 2024
TI  - Can calmodulin bind to lipids of the cytosolic leaflet of plasma membranes?
JF  - Open Biology
VL  - 14
IS  - 9
SP  - 1-8
EP  - 1-8
PB  - ROYAL SOC
SN  - 20462441
KW  - calmodulin
KW  - lipid membrane
KW  - phosphatidylethanolamine
KW  - phosphatidylserine
KW  - calcium
UR  - https://royalsocietypublishing.org/doi/10.1098/rsob.240067
N2  - 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.
ER  -

SCOLLO, Federica; Carmelo TEMPRA; Hueseyin EVCI; Miguel RIOPEDRE-FERNANDEZ; Agnieszka OLZYNSKA; Matti JAVANAINEN; Arunima UDAY; Marek CEBECAUER; Lukasz CWIKLIK; Hector MARTINEZ-SEARA; Pavel JUNGWIRTH; Piotr JURKIEWICZ a Martin HOF. Can calmodulin bind to lipids of the cytosolic leaflet of plasma membranes? \textit{Open Biology}. LONDON: ROYAL SOC, 2024, roč.~14, č.~9, s.~1-8. ISSN~2046-2441. Dostupné z: https://doi.org/10.1098/rsob.240067.

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