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首页> 外文期刊>Molecular and Cellular Biology >The Major Myelin-Resident Protein PLP Is Transported to Myelin Membranes via a Transcytotic Mechanism: Involvement of Sulfatide
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The Major Myelin-Resident Protein PLP Is Transported to Myelin Membranes via a Transcytotic Mechanism: Involvement of Sulfatide

机译：主要的驻留髓磷脂的蛋白PLP通过转细胞机制转运到髓磷脂膜：涉及硫化物

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摘要

Myelin membranes are sheet-like extensions of oligodendrocytes that can be considered membrane domains distinct from the cell's plasma membrane. Consistent with the polarized nature of oligodendrocytes, we demonstrate that transcytotic transport of the major myelin-resident protein proteolipid protein (PLP) is a key element in the mechanism of myelin assembly. Upon biosynthesis, PLP traffics to myelin membranes via syntaxin 3-mediated docking at the apical-surface-like cell body plasma membrane, which is followed by subsequent internalization and transport to the basolateral-surface-like myelin sheet. Pulse-chase experiments, in conjunction with surface biotinylation and organelle fractionation, reveal that following biosynthesis, PLP is transported to the cell body surface in Triton X-100 (TX-100)-resistant microdomains. At the plasma membrane, PLP transiently resides within these microdomains and its lateral dissipation is followed by segregation into 3-[(3-cholamidopropyl)-dimethylammonio]-1-propanesulfonate (CHAPS)-resistant domains, internalization, and subsequent transport toward the myelin membrane. Sulfatide triggers PLP's reallocation from TX-100- into CHAPS-resistant membrane domains, while inhibition of sulfatide biosynthesis inhibits transcytotic PLP transport. Taking these findings together, we propose a model in which PLP transport to the myelin membrane proceeds via a transcytotic mechanism mediated by sulfatide and characterized by a conformational alteration and dynamic, i.e., transient, partitioning of PLP into distinct membrane microdomains involved in biosynthetic and transcytotic transport.
机译：髓磷脂膜是少突胶质细胞的片状延伸，可以认为是与细胞质膜不同的膜结构域。与少突胶质细胞的极化性质一致，我们证明主要的髓磷脂驻留蛋白蛋白脂蛋白（PLP）的跨细胞运输是髓鞘装配机制中的关键要素。在生物合成后，PLP通过语法素3介导的对接在顶表面样细胞质膜上转运到髓磷脂膜，随后被内化并转运到基底外侧表面样髓鞘片。脉冲追踪实验与表面生物素化和细胞器分级分离相结合，揭示了生物合成后，PLP在抗Triton X-100（TX-100）的微区中转运至细胞体表面。在质膜上，PLP暂时驻留在这些微区中，并且其横向耗散之后，分离为对3-[（（3-胆酰胺丙基）-二甲基铵] -1-丙烷磺酸盐（CHAPS）具有抵抗力的区，内化并随后向髓磷脂转运膜。硫化物触发PLP从TX-100-到抗CHAPS的膜结构域的重新分配，而抑制硫化物的生物合成则抑制跨细胞的PLP转运。综合这些发现，我们提出了一个模型，其中PLP通过硫脂介导的胞转机制进行到髓鞘膜的转运，其特征是构象改变和动态（即瞬时）地将PLP划分为参与生物合成和胞转的不同膜微区。运输。

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