alexa Nanoscale distribution of mitochondrial import receptor Tom20 is adjusted to cellular conditions and exhibits an inner-cellular gradient.
Diabetes & Endocrinology

Diabetes & Endocrinology

Journal of Thyroid Disorders & Therapy

Author(s): Wurm CA, Neumann D, Lauterbach MA, Harke B, Egner A, , Wurm CA, Neumann D, Lauterbach MA, Harke B, Egner A,

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Abstract The translocase of the mitochondrial outer membrane (TOM) complex is the main import pore for nuclear-encoded proteins into mitochondria, yet little is known about its spatial distribution within the outer membrane. Super-resolution stimulated emission depletion microscopy was used to determine quantitatively the nanoscale distribution of Tom20, a subunit of the TOM complex, in more than 1,000 cells. We demonstrate that Tom20 is located in clusters whose nanoscale distribution is finely adjusted to the cellular growth conditions as well as to the specific position of a cell within a microcolony. The density of the clusters correlates to the mitochondrial membrane potential. The distributions of clusters of Tom20 and of Tom22 follow an inner-cellular gradient from the perinuclear to the peripheral mitochondria. We conclude that the nanoscale distribution of the TOM complex is finely adjusted to the cellular conditions, resulting in distribution gradients both within single cells and between adjacent cells.
This article was published in Proc Natl Acad Sci U S A and referenced in Journal of Thyroid Disorders & Therapy

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