Journal
AUTOPHAGY
Volume 19, Issue 7, Pages 2151-2152Publisher
TAYLOR & FRANCIS INC
DOI: 10.1080/15548627.2022.2153569
Keywords
Autophagy; drosophila; endoplasmic reticulum-mitochondrial contacts; mitochondrion; phosphatidylinositol-3 kinase
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Miga is an important protein that localizes to the outer membrane of mitochondria and mediates ER-mitochondrial contacts. It regulates phosphatidylinositol-3-phosphate levels and stabilizes proteins involved in autophagy to maintain cellular homeostasis.
Miga is an evolutionarily conserved protein that localizes to the outer membrane of mitochondria and mediates endoplasmic reticulum (ER)-mitochondrial contacts through interaction with VAP proteins in the ER. We recently reported that Miga is required for autophagosome-lysosome fusion during macroautophagy/autophagy. Miga binds to Atg14 and Uvrag, two alternative subunits of the class III phosphatidylinositol 3-kinase (PtdIns3K) complex. Miga regulates phosphatidylinositol-3-phosphate (PtdIns3P) levels through its interaction with Uvrag and its ER-mitochondrial contact site (ERMCS) tethering activity. Miga stabilizes Atg14, which maintains steady levels of the SNARE protein, Syx17. We propose that Miga establishes a direct link between mitochondria and autophagy to maintain cellular homeostasis.
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