Diep Duy Trong Vien, Bohnert Maria
Institute of Cell Dynamics and Imaging, University of Münster, Münster, Germany.
Cells in Motion Interfaculty Centre (CiM), University of Münster, Münster, Germany.
Contact (Thousand Oaks). 2024 Dec 22;7:25152564241308722. doi: 10.1177/25152564241308722. eCollection 2024 Jan-Dec.
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.
脂滴经常与液泡的膜形成接触位点，液泡是酵母中类似溶酶体的细胞器。这些液泡 - 脂滴（vCLIP）接触位点对代谢信号有强烈反应：当营养丰富时，只有一部分脂滴与液泡结合，而其他代谢状态会诱导更强的接触位点形成。脂滴与液泡的物理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接触位点形成和功能的分子基础一直是个谜。当发现vCLIP由结构相关的脂滴系链蛋白Ldo16和Ldo45以及液泡表面蛋白Vac8形成时，这一知识空白得以填补。Ldo45还将磷脂酰肌醇转移蛋白Pdr16招募到vCLIP。在此，我们根据对其分子基础理解的进展回顾有关脂滴 - 液泡接触位点的文献，并讨论该领域的未来方向。
