内膜转移酶
细胞生物学
外膜转位酶
线粒体载体
ATP-ADP转位酶
线粒体内膜
线粒体
蛋白质组
细菌外膜
生物
线粒体膜转运蛋白
膜蛋白
生物化学
膜
基因
大肠杆菌
作者
Zachary N. Wilson,S. Balasubramaniam,Sara Wong,Max-Hinderk Schuler,Mitchell J. Wopat,Adam L. Hughes
标识
DOI:10.1083/jcb.202307036
摘要
The outer mitochondrial membrane (OMM) creates a boundary that imports most of the mitochondrial proteome while removing extraneous or damaged proteins. How the OMM senses aberrant proteins and remodels to maintain OMM integrity remains unresolved. Previously, we identified a mitochondrial remodeling mechanism called the mitochondrial-derived compartment (MDC) that removes a subset of the mitochondrial proteome. Here, we show that MDCs specifically sequester proteins localized only at the OMM, providing an explanation for how select mitochondrial proteins are incorporated into MDCs. Remarkably, selective sorting into MDCs also occurs within the OMM, as subunits of the translocase of the outer membrane (TOM) complex are excluded from MDCs unless assembly of the TOM complex is impaired. Considering that overloading the OMM with mitochondrial membrane proteins or mistargeted tail-anchored membrane proteins induces MDCs to form and sequester these proteins, we propose that one functional role of MDCs is to create an OMM-enriched trap that segregates and sequesters excess proteins from the mitochondrial surface.
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