液泡脂滴接触点vCLIP。

Contact (Thousand Oaks (Ventura County, Calif.)) Pub Date : 2024-12-22 eCollection Date: 2024-01-01 DOI:10.1177/25152564241308722
Duy Trong Vien Diep, Maria Bohnert
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引用次数: 0

摘要

脂滴经常与液泡膜形成接触点,液泡是酵母中的溶酶体样细胞器。这些液泡脂滴(vCLIP)接触位点对代谢线索反应强烈:当营养丰富时,只有一小部分脂滴与液泡结合,其他代谢状态会诱导更强的接触位点形成。物理脂滴-液泡结合与脂噬过程有关,脂噬是一种脂滴特异性的微自噬形式。长期以来,vCLIP接触位点的形成和功能的分子基础仍然是一个谜。当发现vCLIP是由结构相关的脂滴系链蛋白Ldo16和Ldo45以及液泡表面蛋白Vac8组成时,填补了这一知识空白。Ldo45还将磷脂酰肌醇转移蛋白Pdr16募集到vCLIP。本文就脂滴液泡接触位点的分子基础及其研究进展进行综述,并对今后的研究方向进行讨论。
本文章由计算机程序翻译,如有差异,请以英文原文为准。

The Vacuole Lipid Droplet Contact Site vCLIP.

The Vacuole Lipid Droplet Contact Site vCLIP.

The Vacuole Lipid Droplet Contact Site vCLIP.

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

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