title: Mic10 oligomerizes to bend mitochondrial inner membranes at cristae junctions.
abstract: The mitochondrial inner membrane is highly folded and displays a complex molecular architecture. Cristae junctions are highly curved tubular openings that separate cristae membrane invaginations from the surrounding boundary membrane. Despite their central role in many vital cellular processes like apoptosis, the details of cristae junction formation remain elusive. Here we identify Mic10, a core subunit of the recently discovered MICOS complex, as an inner mitochondrial membrane protein with the ability to change membrane morphology in vitro and in vivo. We show that Mic10 spans the inner membrane in a hairpin topology and that its ability to sculpt membranes depends on oligomerization through a glycine-rich motif. Oligomerization mutants fail to induce curvature in model membranes, and when expressed in yeast, mitochondria display an altered inner membrane architecture characterized by drastically decreased numbers of cristae junctions. Thus, we demonstrate that membrane sculpting by Mic10 is essential for cristae junction formation.
authors.affiliation: Department of Cellular Biochemistry, University Medical Center Göttingen, 37073 Göttingen, Germany.
authors.forename: Mariam
authors.initials: M
authors.lastname: Barbot
authors.affiliation: Department of NanoBiophotonics, Max Planck Institute for Biophysical Chemistry, 37077 Göttingen, Germany; Department of Neurology, University Medical Center, 37075 Göttingen, Germany.
authors.forename: Daniel C
authors.initials: DC
authors.lastname: Jans
authors.affiliation: Department of Cellular Biochemistry, University Medical Center Göttingen, 37073 Göttingen, Germany.
authors.forename: Christian
authors.initials: C
authors.lastname: Schulz
authors.affiliation: Department of Cellular Biochemistry, University Medical Center Göttingen, 37073 Göttingen, Germany.
authors.forename: Niels
authors.initials: N
authors.lastname: Denkert
authors.affiliation: Department of Cellular Biochemistry, University Medical Center Göttingen, 37073 Göttingen, Germany.
authors.forename: Benjamin
authors.initials: B
authors.lastname: Kroppen
authors.affiliation: Institute of Microbiology and Genetics, Georg-August-University, 37077 Göttingen, Germany.
authors.forename: Michael
authors.initials: M
authors.lastname: Hoppert
authors.affiliation: Department of NanoBiophotonics, Max Planck Institute for Biophysical Chemistry, 37077 Göttingen, Germany; Department of Neurology, University Medical Center, 37075 Göttingen, Germany.
authors.forename: Stefan
authors.initials: S
authors.lastname: Jakobs
authors.affiliation: Department of Cellular Biochemistry, University Medical Center Göttingen, 37073 Göttingen, Germany; European Neuroscience Institute Göttingen, 37077 Göttingen, Germany. Electronic address: michael.meinecke@med.uni-goettingen.de.
authors.forename: Michael
authors.initials: M
authors.lastname: Meinecke
mesh_terms: D000595:Amino Acid Sequence; D008565:Membrane Proteins / Q000032:analysis / Q000378:metabolism*; D051336:Mitochondrial Membranes / Q000737:chemistry / Q000378:metabolism* / Q000648:ultrastructure; D024101:Mitochondrial Proteins; D008969:Molecular Sequence Data; D055503:Protein Multimerization; D012441:Saccharomyces cerevisiae / Q000737:chemistry / Q000166:cytology* / Q000378:metabolism*; D029701:Saccharomyces cerevisiae Proteins / Q000032:analysis / Q000378:metabolism*; D016415:Sequence Alignment
chemical_list: C573102:MIC10 protein, S cerevisiae; D008565:Membrane Proteins; D024101:Mitochondrial Proteins; D029701:Saccharomyces cerevisiae Proteins