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The mystery of mitochondrial plasticity: TMBIM5 integrates metabolic state and proteostasis
The EMBO Journal ( IF 9.4 ) Pub Date : 2022-08-01 , DOI: 10.15252/embj.2022111834
Mindong Ren 1 , Michael Schlame 1
Affiliation  

How cellular cues alter the mitochondrial proteome and impact the composition of mitochondrial proteins remains poorly understood. In this issue of The EMBO Journal, Patron et al (2022) identify TMBIM5 as an important link between calcium homeostasis, proton motive force, and mitochondrial proteolysis, by which the organelle can modify its protein composition. The results may be crucial for our understanding of the plasticity of mitochondria.

中文翻译:


线粒体可塑性之谜:TMBIM5整合代谢状态和蛋白质稳态



细胞线索如何改变线粒体蛋白质组并影响线粒体蛋白质的组成仍然知之甚少。在本期《EMBO 杂志》中,Patron等人(2022) 认为 TMBIM5 是钙稳态、质子动力和线粒体蛋白水解之间的重要联系,细胞器可以通过它来改变其蛋白质组成。这些结果对于我们理解线粒体的可塑性可能至关重要。
更新日期:2022-08-01
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