Spatio-temporal organization and functionality of OXPHOS complexes seen from the superresolution point of view

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Abstract

ATP synthesis in mitochondria (OXPHOS) is the key for energy supply in most cells. Failure or impairment of this function is closely associated with degenerative processes in diverse neuromuscular or neuronal diseases (Parkinsons disease, Alzheimer). In this context, we aim to understand the spatiotemporal organization of mitochondrial proteins, especially the OXPHOS proteins, in more detail. Recent developments in superresolution microscopy provided new possibilities for precise localization of proteins in cellular compartments. However, only live cell imaging allows for the analysis of the dynamic organization of proteins in situ. We invented Tracking And Localization Microscopy (TALM) (Appelhans et al., NanoLett 2012) of tagged proteins to dissect the spatiotemporal behavior of individual mitochondrial membrane proteins (Tom20, hFis, mitofilin, ATP synthase, Tim23, MPP) in living cells. We were able to show different localization patterns and mobilities of inner and outer membrane proteins as well as matrix proteins. Our results suggest that OXPHOS proteins are trapped in cristae membranes and we provide evidence that the observed confinement is based both on ultrastructural constraints and supercomplex formation.

Speakers from the University of Münster

Busch, Karin

Professur für Zoologie und Molekulare Zellbiologie (Prof. Busch)