Structural implications of mitochondrial dynamics.
Mitochondrial components are continuously distributed throughout the whole chondriome of a cell by fusion and fission. Thus, a single mitochondrion represents a transient fraction of the chondriome. Mitochondrial dynamics are responsible for intracellular distribution and reaction of mitochondria to functional requirements. Dynamics occur on different levels: overall morphology, inner membrane-matrix compartment, turnover and rearrangements of mitochondrial proteins and DNA. Electron micrographs of serial sections of human umbilical vein endothelial cells reveal perinuclear mitochondria of extreme length and with branches in those cells that also have short peripheral mitochondria. Interactions of mitochondria with cytoskeletal elements are revealed in cells treated with cytochalasin D to destroy actin fibrillar structures or after disassembling microtubule by nocodazole. In the latter case mitochondria not only become immobilized, they also acquire a multiple ring structure. In F-actin-disturbed cells, motility (shape changes in particular) is increased and the mitochondria become elongated. Mechanisms of how F-actin might render mitochondria immobile may involve dynamin-related protein 1 (DRP1) or interaction with anion channels. This may be responsible for the lack of mitochondrial motility in senescent cells. Fusion between mitochondria revealed local fluctuations of mitochondrial red fluorescent protein (mtRFP), indicating novel fast inner membrane reorganizations. Mitochondrial dynamics result from a complex interplay between the molecular organization of the inner membrane-matrix complex and cytoskeletal elements outside.
Center of Excellence, Macromolecular Complexes, Institute for Cell Biology and Neurosciences, Johann Wolfgang Goethe University, Frankfurt am Main, Germany. bereiter-hahn@bio.uni-frankfurt.de
Jürgen
J
Bereiter-Hahn
Monika
M
Vöth
Sören
S
Mai
Marina
M
Jendrach
D000818:Animals; D003599:Cytoskeleton / Q000502:physiology* / Q000648:ultrastructure; D005109:Extracellular Matrix / Q000502:physiology* / Q000648:ultrastructure; D006801:Humans; D008928:Mitochondria / Q000502:physiology* / Q000648:ultrastructure; D024101:Mitochondrial Proteins / Q000502:physiology* / Q000648:ultrastructure
D024101:Mitochondrial Proteins