5 research outputs found
The identification and characterization of Mio10 and MINOS1 as novel regulators of mitochondrial inner membrane organization
Various mitochondrial inner membrane
proteins contribute to the structure of cristae membranes and to
the overall dynamic morphology of the inner membrane. These
proteins include the F1FOATPase dimers, which contribute to the
curvature and angular shape of cristae. Also, Fcj1/Mitofilin are
involved in cristae junction formation and act in an antagonistic
manner in inner membrane curvature with respect to F1FOATPase
dimers. Whereas several small proteins mediate F1FOATPase
dimerization in yeast by binding sequentially at monomer
interfaces, the exact nature of what promotes F1FOATPase
dimerization in higher eukaryotes is yet to be determined. To this
end, the initial aim of this study was to identify novel F1FOATPase
dimerization factors in higher eukaryotes that parallel the action
of small dimerization factors in yeast. An in silico approach to
identify novel F1FOATPase dimerization factors resulted in the
identification of the human mitochondrial protein MINOS1 as a
potential candidate. MINOS1, along with its human homolog, Mio10,
were investigated. These proteins however were found not to be
stably associated with the F1FOATPase. Moreover, Mio10 did not
affect F1FOATPase dimerization, oligomerization, or enzymatic
activity. Thus a role of Mio10 and MINOS in dimerization was
excluded. Instead by using an affinity purification based mass
spectrometric analysis, Mio10/MINOS1 were identified as novel
interaction partners of Fcj1/Mitofilin. Topological analysis of
Mio10 and MINOS together with results of size exclusion
chromatography indicated that the two proteins form large
mitochondrial inner membrane complexes. Furthermore, analysis of a
MIO10 deletion strain by fluorescence and electron microscopy
provided evidence for the critical role that Mio10 plays in inner
membrane organization. Mitochondria from mio10â and fcj1â strains
exhibited leaflet-like stacked cristae membranes and appeared to
have lost defined cristae tips. The complex that contains
Mio10/Fcj1 in yeast and MINOS1/Mitofilin in human mitochondria was
hence termed as the MINOS complex (Mitochondrial Inner membrane
Organizing System). The presented findings highlight the functional
and evolutionary significance of the MINOS complex as a player in
mitochondrial inner membrane architecture as well as a
multifunctional component in eukaryotic mitochondria and
potentially in other cellular organelles
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MINOS1 is a conserved component of mitofilin complexes and required for mitochondrial function and cristae organization
MINOS1/Mio10, a conserved mitochondrial protein, is required for mitochondrial inner membrane organization and cristae morphology. MINOS1/Mio10 is a novel constituent of the mitofilin/Fcj1 complex of the inner membrane, linking the morphology phenotype of the mutant to the activity of the mitochondrial inner membrane organizing complex