Shuttling of PINK1 between Mitochondrial Microcompartments Resolved by Triple-Color Superresolution Microscopy

Autor(en): Beinlich, Felix R. M.
Drees, Christoph
Piehler, Jacob 
Busch, Karin B.
Stichwörter: Biochemistry & Molecular Biology; CLEAVAGE; COMPLEX; IMPORT; KINASE; MEMBRANE; MITOPHAGY; ORGANIZATION; PATHWAY; PROTEINS; TRACKING
Erscheinungsdatum: 2015
Herausgeber: AMER CHEMICAL SOC
Journal: ACS CHEMICAL BIOLOGY
Volumen: 10
Ausgabe: 9
Startseite: 1970
Seitenende: 1976
Zusammenfassung: 
The cytosolic phosphatase and tensin homologue Pten-kinase PINK1 involved in mitochondrial quality control undergoes a proteolytic process inside mitochondria. It has been suggested that the protein is not fully imported into mitochondria during this maturation. Here, we have established live cell triple-color superresolution microscopy by combining FPALM and tracking and localization microscopy (TALM) in order to unravel the spatiotemporal organization of the C-terminal kinase domain of PINKI during this process. We find that the kinase domain is imported into active mitochondria and colocalizes with respiratory complex I at the inner mitochondrial membrane. When the processing step inside mitochondria is inhibited or mitochondria are de-energized, full length PINK1 distributes between the outer and the inner mitochondrial membranes, indicating a holdup of import. These findings give the molecular base for a dual role of PINK1-inside energized mitochondria and outside of de-energized mitochondria.
ISSN: 15548929
DOI: 10.1021/acschembio.5b00295

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