AI Article Synopsis
- The endoplasmic reticulum (ER) closely interacts with mitochondria, with the protein FUNDC1 helping to recruit Drp1 for mitochondrial division, especially under low oxygen (hypoxic) conditions.
- Researchers found that USP19, a protein located in the ER, gathers at ER-mitochondria contact sites during hypoxia and aids in the process of mitochondrial fission.
- USP19 works by binding to and modifying FUNDC1, enhancing Drp1's ability to promote mitochondrial division, thereby uncovering a new pathway for how the ER regulates mitochondrial behavior during low-oxygen stress.
Article Abstract
The ER tethers tightly to mitochondria and the mitochondrial protein FUNDC1 recruits Drp1 to ER-mitochondria contact sites, subsequently facilitating mitochondrial fission and preventing mitochondria from undergoing hypoxic stress. However, the mechanisms by which the ER modulates hypoxia-induced mitochondrial fission are poorly understood. Here, we show that USP19, an ER-resident deubiquitinase, accumulates at ER-mitochondria contact sites under hypoxia and promotes hypoxia-induced mitochondrial division. In response to hypoxia, USP19 binds to and deubiquitinates FUNDC1 at ER-mitochondria contact sites, which facilitates Drp1 oligomerization and Drp1 GTP-binding and hydrolysis activities, thereby promoting mitochondrial division. Our findings reveal a unique hypoxia response pathway mediated by an ER protein that regulates mitochondrial dynamics.
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Source |
|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC8127008 | PMC |
| http://dx.doi.org/10.1083/jcb.202010006 | DOI Listing |
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