线粒体对接蛋白亲突蛋白在少突胶质细胞和中枢神经系统髓鞘中的表达和亚细胞定位,Glia

当前位置： X-MOL 学术 › Glia › 论文详情

Our official English website, www.x-mol.net, welcomes your feedback! (Note: you will need to create a separate account there.)

线粒体对接蛋白亲突蛋白在少突胶质细胞和中枢神经系统髓鞘中的表达和亚细胞定位
Glia ( IF 6.2 ) Pub Date : 2023-06-05 , DOI: 10.1002/glia.24425
Diane S Nakamura ₁ , Jean-David M Gothié ₁ , Samantha F Kornfeld _{2,

3} , Rashmi Kothary _{2,

3,

4,

5} , Timothy E Kennedy ₁

Affiliation

少突胶质细胞产生富含脂质的髓鞘，为下面的轴突提供代谢支持并促进跳跃传导。少突胶质细胞线粒体提供脂质合成所需的大量能量和碳链主链。髓鞘中线粒体的稀疏性表明，线粒体运输的严格调节对于线粒体在细胞中的有效分布至关重要。特别是，线粒体在轴神经胶质连接处的保留将支持髓鞘形成过程中的局部脂质合成和膜重塑。少突胶质细胞中的线粒体对接是如何调节的尚不清楚。我们的研究结果表明，syntaphilin (SNPH) 是一种在神经元中表征的线粒体对接蛋白，在体外由少突胶质细胞前体细胞 (OPC) 和成熟少突胶质细胞表达，并存在于体内髓鞘中。我们之前曾报道过，netrin-1 的浴应用促进了髓磷脂碱性蛋白阳性膜的形成，并且 netrin-1 包被微珠的局部呈现导致线粒体在少突胶质细胞珠粘附部位快速积累。在这里，我们发现，在髓磷脂碱性蛋白阳性膜扩张过程中，netrin-1 增加了 SNPH 向少突胶质细胞过程的重新分配，并且 SNPH 在少突胶质细胞质膜上与 netrin-1 包被的珠子粘附的位点处聚集，其中线粒体被保留。这些发现表明 SNPH 在少突胶质细胞中调节 netrin-1 介导的线粒体对接和髓磷脂膜扩张的作用。

"点击查看英文标题和摘要"

Expression and subcellular localization of mitochondrial docking protein, syntaphilin, in oligodendrocytes and CNS myelin sheath

Oligodendrocytes produce lipid-rich myelin sheaths that provide metabolic support to the underlying axon and facilitate saltatory conduction. Oligodendrocyte mitochondria supply the bulk of energy and carbon-chain backbones required for lipid synthesis. The sparsity of mitochondria in the myelin sheath suggests that tight regulation of mitochondrial trafficking is crucial for their efficient distribution in the cell. In particular, retention of mitochondria at axoglial junctions would support local lipid synthesis and membrane remodeling during myelination. How mitochondrial docking in oligodendrocytes is regulated is not known. Our findings indicate that syntaphilin (SNPH), a mitochondrial docking protein that has been characterized in neurons, is expressed by oligodendrocyte precursor cells (OPCs) and mature oligodendrocytes in vitro and present in the myelin sheath in vivo. We have previously reported that bath application of netrin-1 promotes the elaboration of myelin basic protein-positive membranes, and that localized presentation of a netrin-1 coated microbead results in rapid accumulation of mitochondria at the site of oligodendrocyte-bead adhesion. Here we show that netrin-1 increases the redistribution of SNPH to oligodendrocyte processes during the expansion of myelin basic protein-positive membranes and that SNPH clusters at the oligodendrocyte plasma membrane at sites of adhesion with netrin-1-coated beads where mitochondria are retained. These findings suggest roles for SNPH in oligodendrocytes regulating netrin-1-mediated mitochondrial docking and myelin membrane expansion.

更新日期：2023-06-05

点击分享查看原文

点击收藏

公开下载

阅读更多本刊最新论文本刊介绍/投稿指南

全部期刊列表>>