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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geprüft am 03.05.2024