Open AccessMSTO 1 is a cytoplasmic pro‐mitochondrial fusion protein
Author(s) -
Gal Aniko,
Balicza Peter,
Weaver David,
Naghdi Shamim,
Joseph Suresh K,
Várnai Péter,
Gyuris Tibor,
Horváth Attila,
Nagy Laszlo,
Seifert Erin L,
Molnar Maria Judit,
Hajnóczky György
Publication year - 2017
Publication title -
embo molecular medicine
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.923
H-Index - 107
eISSN - 1757-4684
pISSN - 1757-4676
DOI - 10.15252/emmm.201607058
Subject(s) - mitochondrion , cytoplasm , colocalization , microbiology and biotechnology , mitochondrial fusion , biology , chemistry , biochemistry , mitochondrial dna , gene
The protein MSTO 1 has been localized to mitochondria and linked to mitochondrial morphology, but its specific role has remained unclear. Lactate stress test and myopathological results suggest mitochondrial dysfunction. In patient fibroblasts, MSTO 1 mRNA and protein abundance are decreased, mitochondria display fragmentation, aggregation, and decreased network continuity and fusion activity. Short‐term silencing of MSTO 1 in HeLa cells reproduced the impairment of mitochondrial morphology and dynamics observed in the fibroblasts without damaging bioenergetics. At variance with a previous report, we find MSTO 1 to be localized in the cytoplasmic area with limited colocalization with mitochondria. MSTO 1 interacts with the fusion machinery as a soluble factor at the cytoplasm‐mitochondrial outer membrane interface. After plasma membrane permeabilization, MSTO 1 is released from the cells. MSTO 1 likely has a physiologically relevant role in mitochondrial morphogenesis by supporting mitochondrial fusion. §