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2015 ; 35
(24
): 4222-37
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The Oxidation Status of Mic19 Regulates MICOS Assembly
#MMPMID26416881
Sakowska P
; Jans DC
; Mohanraj K
; Riedel D
; Jakobs S
; Chacinska A
Mol Cell Biol
2015[Dec]; 35
(24
): 4222-37
PMID26416881
show ga
The function of mitochondria depends on the proper organization of mitochondrial
membranes. The morphology of the inner membrane is regulated by the recently
identified mitochondrial contact site and crista organizing system (MICOS)
complex. MICOS mutants exhibit alterations in crista formation, leading to
mitochondrial dysfunction. However, the mechanisms that underlie MICOS regulation
remain poorly understood. MIC19, a peripheral protein of the inner membrane and
component of the MICOS complex, was previously reported to be required for the
proper function of MICOS in maintaining the architecture of the inner membrane.
Here, we show that human and Saccharomyces cerevisiae MIC19 proteins undergo
oxidation in mitochondria and require the mitochondrial intermembrane space
assembly (MIA) pathway, which couples the oxidation and import of mitochondrial
intermembrane space proteins for mitochondrial localization. Detailed analyses
identified yeast Mic19 in two different redox forms. The form that contains an
intramolecular disulfide bond is bound to Mic60 of the MICOS complex. Mic19
oxidation is not essential for its integration into the MICOS complex but plays a
role in MICOS assembly and the maintenance of the proper inner membrane
morphology. These findings suggest that Mic19 is a redox-dependent regulator of
MICOS function.
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