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

Felix R.M. Beinlich, Christoph Drees, Jacob Piehler, Karin B Busch

13 Citationer (Scopus)

Abstract

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.

OriginalsprogEngelsk
TidsskriftA C S Chemical Biology
Vol/bind10
Udgave nummer9
Sider (fra-til)1970-1976
Antal sider7
ISSN1554-8929
DOI
StatusUdgivet - 18 sep. 2015
Udgivet eksterntJa

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