A possible role for VPS13-family proteins in bulk lipid transfer, membrane expansion and organelle biogenesis.

A possible role for VPS13-family proteins in bulk lipid transfer, membrane expansion and organelle biogenesis.
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DOI:
10.1242/jcs.259357
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发表时间:
2022-03-01
影响因子:
4
通讯作者:
Reinisch KM
Reinisch KM
中科院分区:
生物学2区
文献类型:
--
作者:
Melia TJ;Reinisch KM

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在细胞器-细胞器接触部位,蛋白质促进脂质的快速运动早已为人所知。典型地,这种脂质转运涉及将单个脂质提取到脂质转运蛋白上的疏水性口袋中。最近,一类新的脂质转运蛋白被描述为具有物理特性,表明这些蛋白可能具有不同的功能。它们具有很长的疏水束,可以一次结合许多脂质,并在接触部位跨越膜之间的整个鸿沟,这表明它们可能作为促进大量脂质流动的桥梁。在这里,我们回顾了这类脂质转运蛋白的结构和功能,其中最具特征的成员是VPS13和ATG2蛋白,以及它们与细胞器膜上其他脂质动员蛋白的明显协调。我们还讨论了该领域的主流假设,即这种类型的脂质转运可能通过脂质的大量递送促进膜扩张,以及围绕这些新型脂质转运蛋白的其他新出现的假设和问题。摘要:我们讨论了vps13家族蛋白在细胞器间囊泡非依赖性散装脂质运输中的新作用,这种运输的可能功能和潜在的分子机制。
At organelle–organelle contact sites, proteins have long been known to facilitate the rapid movement of lipids. Classically, this lipid transport involves the extraction of single lipids into a hydrophobic pocket on a lipid transport protein. Recently, a new class of lipid transporter has been described with physical characteristics that suggest these proteins are likely to function differently. They possess long hydrophobic tracts that can bind many lipids at once and physically span the entire gulf between membranes at contact sites, suggesting that they may act as bridges to facilitate bulk lipid flow. Here, we review what has been learned regarding the structure and function of this class of lipid transporters, whose best characterized members are VPS13 and ATG2 proteins, and their apparent coordination with other lipid-mobilizing proteins on organelle membranes. We also discuss the prevailing hypothesis in the field, that this type of lipid transport may facilitate membrane expansion through the bulk delivery of lipids, as well as other emerging hypotheses and questions surrounding these novel lipid transport proteins. Summary: We discuss emerging roles of VPS13-family proteins in vesicle-independent bulk lipid transport between organelles, the possible functions of such transport and the underlying molecular mechanisms.
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