Insertases scramble lipids: Molecular simulations of MTCH2

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Publikace nespadá pod Filozofickou fakultu, ale pod Středoevropský technologický institut. Oficiální stránka publikace je na webu muni.cz.
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BARTOŠ Ladislav MENON Anant K. VÁCHA Robert

Rok publikování 2024
Druh Článek v odborném periodiku
Časopis / Zdroj Structure
Fakulta / Pracoviště MU

Středoevropský technologický institut

Citace
www https://www.sciencedirect.com/science/article/pii/S0969212624000364?via%3Dihub
Doi http://dx.doi.org/10.1016/j.str.2024.01.012
Klíčová slova flip-flop rate; free energy barrier; hydrophilic groove; insertase; membrane defect; molecular dynamics; scramblase
Přiložené soubory
Popis Scramblases play a pivotal role in facilitating bidirectional lipid transport across cell membranes, thereby influencing lipid metabolism, membrane homeostasis, and cellular signaling. MTCH2, a mitochondrial outer membrane protein insertase, has a membrane-spanning hydrophilic groove resembling those that form the lipid transit pathway in known scramblases. Employing both coarse-grained and atomistic molecular dynamics simulations, we show that MTCH2 significantly reduces the free energy barrier for lipid movement along the groove and therefore can indeed function as a scramblase. Notably, the scrambling rate of MTCH2 in silico is similar to that of voltage-dependent anion channel (VDAC), a recently discovered scramblase of the outer mitochondrial membrane, suggesting a potential complementary physiological role for these mitochondrial proteins. Finally, our findings suggest that other insertases which possess a hydrophilic path across the membrane like MTCH2, can also function as scramblases.
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