Shuttling of PINK1 between Mitochondrial Microcompartments Resolved by Triple-Color Superresolution Microscopy
Research output: Contribution to journal › Letter › Research › peer-review
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 super-resolution microscopy by combining FPALM and tracking and localization microscopy (TALM) in order to unravel the spatiotemporal organization of the C-terminal kinase domain of PINK1 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.
Original language | English |
---|---|
Journal | A C S Chemical Biology |
Volume | 10 |
Issue number | 9 |
Pages (from-to) | 1970-1976 |
Number of pages | 7 |
ISSN | 1554-8929 |
DOIs | |
Publication status | Published - 2015 |
Externally published | Yes |
- HeLa Cells, Humans, Membrane Potential, Mitochondrial, Microscopy, Fluorescence, Mitochondria/metabolism, Mitochondrial Membranes/metabolism, Protein Kinases/analysis, Protein Structure, Tertiary
Research areas
ID: 209744399