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首页> 外文期刊>The EMBO journal. >Proteasomal degradation induced by DPP9-mediated processing competes with mitochondrial protein import
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Proteasomal degradation induced by DPP9-mediated processing competes with mitochondrial protein import

机译：蛋白酶体降解DPP9-mediated引起的处理与线粒体蛋白质竞争进口

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摘要

Plasticity of the proteome is critical to adapt to varying conditions. Control of mitochondrial protein import contributes to this plasticity. Here, we identified a pathway that regulates mitochondrial protein import by regulated N-terminal processing. We demonstrate that dipeptidyl peptidases 8/9 (DPP8/9) mediate the N-terminal processing of adenylate kinase 2 (AK2) en route to mitochondria. We show that AK2 is a substrate of the mitochondrial disulfide relay, thus lacking an N-terminal mitochondrial targeting sequence and undergoing comparatively slow import. DPP9-mediated processing of AK2 induces its rapid proteasomal degradation and prevents cytosolic accumulation of enzymatically active AK2. Besides AK2, we identify more than 100 mitochondrial proteins with putative DPP8/9 recognition sites and demonstrate that DPP8/9 influence the cellular levels of a number of these proteins. Collectively, we provide in this study a conceptual framework on how regulated cytosolic processing controls levels of mitochondrial proteins as well as their dual localization to mitochondria and other compartments.
机译：蛋白质组的可塑性适应至关重要不同的条件。蛋白质进口有助于这种可塑性。在这里,我们发现了一个调节的通路线粒体蛋白进口管制氨基端处理。dipeptidyl肽酶(DPP8/9)调解8/9氨基端处理腺苷酸激酶2 (AK2)途中线粒体。二硫化线粒体继电器的衬底,因此缺乏一个氨基端线粒体针对序列并进行比较缓慢的进口。其快速的蛋白酶体降解和诱导防止胞质酶积累AK2活跃。100年线粒体蛋白质与假定的DPP8/9网站和证明DPP8/9认可细胞水平的影响这些蛋白质。研究一个概念性的框架如何监管胞质处理控制的水平线粒体蛋白质及其对偶线粒体和本地化隔间。

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