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Journal Article

STED super-resolution microscopy reveals an array of MINOS clusters along human mitochondria.

MPS-Authors
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Jans,  D. C.
Research Group of Mitochondrial Structure and Dynamics, MPI for biophysical chemistry, Max Planck Society;

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Wurm,  C. A.
Department of NanoBiophotonics, MPI for biophysical chemistry, Max Planck Society;

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Riedel,  D.
Facility for Electron Microscopy, MPI for biophysical chemistry, Max Planck Society;

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Wenzel,  D.
Facility for Electron Microscopy, MPI for biophysical chemistry, Max Planck Society;

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Stagge,  F.
Department of NanoBiophotonics, MPI for biophysical chemistry, Max Planck Society;

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Jakobs,  S.
Research Group of Mitochondrial Structure and Dynamics, MPI for biophysical chemistry, Max Planck Society;

External Ressource
Fulltext (public)

1824807.pdf
(Publisher version), 1021KB

Supplementary Material (public)

1824807_Supplement_I.pdf
(Supplementary material), 716KB

1824807_Supplement_2.ppt
(Supplementary material), 227KB

1824807_Supplement_3.ppt
(Supplementary material), 177KB

1824807_Supplement_4.ppt
(Supplementary material), 233KB

1824807_Supplemet_5.ppt
(Supplementary material), 325KB

1824807_Supplement_6.ppt
(Supplementary material), 273KB

1824807_Supplement_7.ppt
(Supplementary material), 497KB

Citation

Jans, D. C., Wurm, C. A., Riedel, D., Wenzel, D., Stagge, F., Deckers, M., et al. (2013). STED super-resolution microscopy reveals an array of MINOS clusters along human mitochondria. Proceedings of the National Academy of Sciences of the United States of America, 110(22), 8936-8941. doi:10.1073/pnas.1301820110.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0014-1AB5-6
Abstract
The mitochondrial inner membrane organizing system (MINOS) is a conserved large hetero-oligomeric protein complex in the mitochondrial inner membrane, crucial for the maintenance of cristae morphology. MINOS has been suggested to represent the core of an extended protein network that controls mitochondrial function and structure, and has been linked to several human diseases. The spatial arrangement of MINOS within mitochondria is ill-defined, however. Using super-resolution stimulated emission depletion (STED) microscopy and immunogold electron microscopy, we determined the distribution of three known human MINOS subunits (mitofilin, MINOS1, and CHCHD3) in mammalian cells. Super-resolution microscopy revealed that all three subunits form similar clusters within mitochondria, and that MINOS is more abundant in mitochondria around the nucleus than in peripheral mitochondria. At the submitochondrial level, mitofilin, a core MINOS subunit, is preferentially localized at cristae junctions. In primary human fibroblasts, mitofilin labeling uncovered a regularly spaced pattern of clusters arranged in parallel to the cell growth surfaces. We suggest that this array of MINOS complexes might explain the observed phenomenon of largely horizontally arranged cristae junctions that connect the inner boundary membrane to lamellar cristae. The super-resolution images demonstrate an unexpectedly high level of regularity in the nanoscale distribution of the MINOS complex in human mitochondria, supporting an integrating role of MINOS in the structural organization of the organelle.