Ohba, Yohsuke, MacVicar, Thomas and Langer, Thomas (2020). Regulation of mitochondrial plasticity by the i-AAA protease YME1L. Biol. Chem., 401 (6-7). S. 877 - 891. BERLIN: WALTER DE GRUYTER GMBH. ISSN 1437-4315

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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.

Item Type: Journal Article
Creators:
CreatorsEmailORCIDORCID Put Code
Ohba, YohsukeUNSPECIFIEDUNSPECIFIEDUNSPECIFIED
MacVicar, ThomasUNSPECIFIEDUNSPECIFIEDUNSPECIFIED
Langer, ThomasUNSPECIFIEDUNSPECIFIEDUNSPECIFIED
URN: urn:nbn:de:hbz:38-334798
DOI: 10.1515/hsz-2020-0120
Journal or Publication Title: Biol. Chem.
Volume: 401
Number: 6-7
Page Range: S. 877 - 891
Date: 2020
Publisher: WALTER DE GRUYTER GMBH
Place of Publication: BERLIN
ISSN: 1437-4315
Language: English
Faculty: Unspecified
Divisions: Unspecified
Subjects: no entry
Uncontrolled Keywords:
KeywordsLanguage
QUALITY-CONTROL; PROTEOLYTIC CLEAVAGE; CELL-PROLIFERATION; TUMOR-SUPPRESSOR; OPA1 ISOFORMS; LON PROTEASE; DEGRADATION; FUSION; DEATH; OMA1Multiple languages
Biochemistry & Molecular BiologyMultiple languages
URI: http://kups.ub.uni-koeln.de/id/eprint/33479

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