The Vacuole Lipid Droplet Contact Site vCLIP DOI Creative Commons
Duy Trong Vien Diep, Maria Bohnert

Contact, Год журнала: 2024, Номер 7

Опубликована: Янв. 1, 2024

Lipid droplets frequently form contact sites with the membrane of vacuole, lysosome-like organelle in yeast. These vacuole lipid droplet (vCLIP) respond strongly to metabolic cues: while only a subset is bound when nutrients are abundant, other states induce stronger site formation. Physical droplet-vacuole binding related process lipophagy, droplet-specific microautophagy. The molecular basis for formation and function vCLIP remained enigmatic long time. This knowledge gap was filled it found that formed by structurally tether proteins Ldo16 Ldo45, vacuolar surface protein Vac8. Ldo45 additionally recruits phosphatidylinositol transfer Pdr16 vCLIP. Here, we review literature on light progress our understanding its discuss future directions field.

Язык: Английский

Modulating lipid droplet dynamics in neurodegeneration: an emerging area of molecular pharmacology DOI

RS Verma,

Prateek Sharma, Veerta Sharma

и другие.

Molecular Biology Reports, Год журнала: 2025, Номер 52(1)

Опубликована: Март 3, 2025

Язык: Английский

Процитировано

0
Recent advances in fluorescent probes for bioimaging lipid droplets associated diseases DOI

Wenli Jiang,

Kexin Du, Jing Zhang

и другие.

Dyes and Pigments, Год журнала: 2025, Номер unknown, С. 112792 - 112792

Опубликована: Март 1, 2025

Язык: Английский

Процитировано

0
Substrates (Acyl‐CoA and Diacylglycerol) Entry and Products (CoA and Triacylglycerol) Egress Pathways in DGAT1 DOI Creative Commons
Hwa-Young Lee, Wonpil Im

Journal of Computational Chemistry, Год журнала: 2025, Номер 46(11)

Опубликована: Апрель 19, 2025

ABSTRACT Diacylglycerol O‐acyltransferase 1 (DGAT1) is an integral membrane protein that uses acyl‐coenzyme A (acyl‐CoA) and diacylglycerol (DAG) to catalyze the formation of triacylglycerides (TAGs). The acyl transfer reaction occurs between activated carboxylate group fatty acid free hydroxyl on glycerol backbone DAG. However, how two substrates enter DGAT1's catalytic chamber interact with DGAT1 remains elusive. This study aims explore structural basis substrate recognition by investigating each substrate's pathway chamber. Using a human cryo‐EM structure in complex oleoyl‐CoA substrate, we designed different all‐atom molecular dynamics (MD) simulation systems: away (both acyl‐CoA DAG from chamber) bound (acyl‐CoA chamber). Our simulations reveal approaches via interactions positively charged residues transmembrane helix 7. show DAGs entering into cytosol leaflet. acyl‐CoA's lines up headgroup DAG, which appears be competent TAG formation. We then converted them coenzyme (CoA) used adaptive biasing force (ABF) egress pathways products. identify their escape routes, are aligned respective entry pathways. Visualization product expected guide future experimental design better understand function.

Язык: Английский

Процитировано

0
The Vacuole Lipid Droplet Contact Site vCLIP DOI Creative Commons
Duy Trong Vien Diep, Maria Bohnert

Contact, Год журнала: 2024, Номер 7

Опубликована: Янв. 1, 2024

Lipid droplets frequently form contact sites with the membrane of vacuole, lysosome-like organelle in yeast. These vacuole lipid droplet (vCLIP) respond strongly to metabolic cues: while only a subset is bound when nutrients are abundant, other states induce stronger site formation. Physical droplet-vacuole binding related process lipophagy, droplet-specific microautophagy. The molecular basis for formation and function vCLIP remained enigmatic long time. This knowledge gap was filled it found that formed by structurally tether proteins Ldo16 Ldo45, vacuolar surface protein Vac8. Ldo45 additionally recruits phosphatidylinositol transfer Pdr16 vCLIP. Here, we review literature on light progress our understanding its discuss future directions field.

Язык: Английский

Процитировано

0