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Regulation of mitochondrial plasticity by the i-AAA protease YME1L

Authors
  • Ohba, Yohsuke1
  • MacVicar, Thomas1
  • Langer, Thomas1, 2
  • 1 Max Planck Institute for Biology of Ageing, Joseph-Stelzmann-Str. 9b , (Germany)
  • 2 University of Cologne, Germany , (Germany)
Type
Published Article
Journal
Biological Chemistry
Publisher
Walter de Gruyter GmbH
Publication Date
May 26, 2020
Volume
401
Issue
6-7
Pages
877–890
Identifiers
DOI: 10.1515/hsz-2020-0120
Source
De Gruyter
Keywords
License
Yellow

Abstract

Mitochondria are multifaceted metabolic organelles and adapt dynamically to various developmental transitions and environmental challenges. The metabolic flexibility of mitochondria is provided by alterations in the mitochondrial proteome and is tightly coupled to changes in the shape of mitochondria. Mitochondrial proteases are emerging as important posttranslational regulators of mitochondrial plasticity. The i-AAA protease YME1L, an ATP-dependent proteolytic complex in the mitochondrial inner membrane, coordinates mitochondrial biogenesis and dynamics with the metabolic output of mitochondria. mTORC1-dependent lipid signaling drives proteolytic rewiring of mitochondria by YME1L. While the tissue-specific loss of YME1L in mice is associated with heart failure, disturbed eye development, and axonal degeneration in the spinal cord, YME1L activity supports growth of pancreatic ductal adenocarcinoma cells. YME1L thus represents a key regulatory protease determining mitochondrial plasticity and metabolic reprogramming and is emerging as a promising therapeutic target.

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