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  Acylglycerol Kinase Mutated in Sengers Syndrome Is a Subunit of the TIM22 Protein Translocase in Mitochondria

Vukotic, M., Nolte, H., Konig, T., Saita, S., Ananjew, M., Kruger, M., et al. (2017). Acylglycerol Kinase Mutated in Sengers Syndrome Is a Subunit of the TIM22 Protein Translocase in Mitochondria. Mol Cell, 67(3), 471-483 e7. doi:10.1016/j.molcel.2017.06.013.

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Item Permalink: https://hdl.handle.net/21.11116/0000-0001-593C-9 Version Permalink: https://hdl.handle.net/21.11116/0000-0001-593D-8
Genre: Journal Article

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https://www.ncbi.nlm.nih.gov/pubmed/28712724 (Any fulltext)
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Vukotic, M.1, Author
Nolte, H.1, Author
Konig, T.1, Author
Saita, S.1, Author
Ananjew, M.1, Author
Kruger, M.1, Author
Tatsuta, T.1, Author
Langer, T.1, Author
Affiliations:
1Max Planck Institute for Biology of Ageing, Max Planck Society, Joseph-Stelzmann-Str. 9b, D-50931 Cologne, DE, ou_1942284              

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Free keywords: Adenine Nucleotide Translocator 1/metabolism Antiporters/metabolism Apoptosis Calcium-Binding Proteins/metabolism Cardiomyopathies/*enzymology/genetics/pathology Cataract/*enzymology/genetics/pathology Genetic Predisposition to Disease HEK293 Cells HeLa Cells Humans Mitochondria/*enzymology/pathology Mitochondrial Membrane Transport Proteins/genetics/*metabolism Mitochondrial Proteins/metabolism Multiprotein Complexes Mutation Phenotype Phospholipids/metabolism Phosphotransferases (Alcohol Group Acceptor)/genetics/*metabolism Protein Transport Time Factors Transfection Sengers syndrome TIM22 complex acylglycerol kinase cardiolipin cristae mitochondria mitochondrial protein import phosphatidic acid
 Abstract: Mutations in mitochondrial acylglycerol kinase (AGK) cause Sengers syndrome, which is characterized by cataracts, hypertrophic cardiomyopathy, and skeletal myopathy. AGK generates phosphatidic acid and lysophosphatidic acid, bioactive phospholipids involved in lipid signaling and the regulation of tumor progression. However, the molecular mechanisms of the mitochondrial pathology remain enigmatic. Determining its mitochondrial interactome, we have identified AGK as a constituent of the TIM22 complex in the mitochondrial inner membrane. AGK assembles with TIMM22 and TIMM29 and supports the import of a subset of multi-spanning membrane proteins. The function of AGK as a subunit of the TIM22 complex does not depend on its kinase activity. However, enzymatically active AGK is required to maintain mitochondrial cristae morphogenesis and the apoptotic resistance of cells. The dual function of AGK as lipid kinase and constituent of the TIM22 complex reveals that disturbances in both phospholipid metabolism and mitochondrial protein biogenesis contribute to the pathogenesis of Sengers syndrome.

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 Dates: 2017
 Publication Status: Issued
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 Rev. Type: -
 Identifiers: Other: 28712724
DOI: 10.1016/j.molcel.2017.06.013
ISSN: 1097-4164 (Electronic)1097-2765 (Linking)
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Title: Mol Cell
Source Genre: Journal
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Pages: - Volume / Issue: 67 (3) Sequence Number: - Start / End Page: 471 - 483 e7 Identifier: -