title: Cristae formation-linking ultrastructure and function of mitochondria.
abstract: Mitochondria are double-membrane enclosed eukaryotic organelles with a central role in numerous cellular functions. The ultrastructure of mitochondria varies considerably between tissues, organisms, and the physiological state of cells. Alterations and remodeling of inner membrane structures are evident in numerous human disorders and during apoptosis. The inner membrane is composed of two subcompartments, the cristae membrane and the inner boundary membrane. Recent advances in electron tomography led to the current view that these membrane domains are connected by rather small tubular structures, termed crista junctions. They have been proposed to regulate the dynamic distribution of proteins and lipids as well as of soluble metabolites between individual mitochondrial subcompartments. One example is the release of cytochrome c upon induction of apoptosis. However, only little is known on the molecular mechanisms mediating the formation and maintenance of cristae and crista junctions. Here we review the current knowledge of the factors that determine cristae morphology and how the latter is linked to mitochondrial function. Further, we formulate several theoretical models which could account for the de novo formation of cristae as well as their propagation from existing cristae.
authors.affiliation: Adolf-Butenandt-Institut für Physiologische Chemie, Ludwig-Maximilians-Universität München, Butenandtstr. 5, 81377 München, Germany.
authors.forename: Michael
authors.initials: M
authors.lastname: Zick
authors.forename: Regina
authors.initials: R
authors.lastname: Rabl
authors.forename: Andreas S
authors.initials: AS
authors.lastname: Reichert
mesh_terms: D017209:Apoptosis; D004734:Energy Metabolism; D006801:Humans; D008928:Mitochondria / Q000378:metabolism* / Q000648:ultrastructure*; D051336:Mitochondrial Membranes / Q000502:physiology* / Q000648:ultrastructure; D024101:Mitochondrial Proteins / Q000378:metabolism; D025261:Mitochondrial Proton-Translocating ATPases / Q000378:metabolism; D008954:Models, Biological; D010300:Parkinson Disease / Q000378:metabolism
chemical_list: D024101:Mitochondrial Proteins; C474451:F1F0-ATP synthase; D025261:Mitochondrial Proton-Translocating ATPases