Central role of mic10 in the mitochondrial contact site and cristae organizing system

Bohnert, M., Zerbes, R. M., Davies, K. M., Mühleip, A. W., Rampelt, H., Horvath, S. E., Boenke, T., Kram, A., Perschil, I., Veenhuis, M., Kühlbrandt, W., van der Klei, I. J., Pfanner, N. & van der Laan, M., 5-May-2015, In : Cell metabolism. 21, 5, p. 747-755 9 p.

Research output: Contribution to journalArticleAcademicpeer-review

  • Maria Bohnert
  • Ralf M Zerbes
  • Karen M Davies
  • Alexander W Mühleip
  • Heike Rampelt
  • Susanne E Horvath
  • Thorina Boenke
  • Anita Kram
  • Inge Perschil
  • Marten Veenhuis
  • Werner Kühlbrandt
  • Ida J van der Klei
  • Nikolaus Pfanner
  • Martin van der Laan

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.

Original languageEnglish
Pages (from-to)747-755
Number of pages9
JournalCell metabolism
Issue number5
Publication statusPublished - 5-May-2015

Download statistics

No data available

ID: 19671420