Abstract：
:The mitochondrial contact site and cristae organizing system (MICOS) is a conserved multi-subunit complex crucial for maintaining the characteristic architecture of mitochondria. Studies with deletion mutants identified Mic10 and Mic60 as core subunits of MICOS. Mic60 has been studied in detail; however, topogenesis and function of Mic10 are unknown. We report that targeting of Mic10 to the mitochondrial inner membrane requires a positively charged internal loop, but no cleavable presequence. Both transmembrane segments of Mic10 carry a characteristic four-glycine motif, which has been found in the ring-forming rotor subunit of F1Fo-ATP synthases. Overexpression of Mic10 profoundly alters the architecture of the inner membrane independently of other MICOS components. The four-glycine motifs are dispensable for interaction of Mic10 with other MICOS subunits but are crucial for the formation of large Mic10 oligomers. Our studies identify a unique role of Mic10 oligomers in promoting the formation of inner membrane crista junctions.
journal_name
Cell Metabjournal_title
Cell metabolismauthors
Bohnert M,Zerbes RM,Davies KM,Mühleip AW,Rampelt H,Horvath SE,Boenke T,Kram A,Perschil I,Veenhuis M,Kühlbrandt W,van der Klei IJ,Pfanner N,van der Laan Mdoi
10.1016/j.cmet.2015.04.007subject
Has Abstractpub_date
2015-05-05 00:00:00pages
747-55issue
5eissn
1550-4131issn
1932-7420pii
S1550-4131(15)00162-Xjournal_volume
21pub_type
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