Studies on the interaction between mitochondria and the cytoskeleton.
Mitochondrial movements and morphology are regulated through interactions with the cytoskeletal system, in particular the microtubules. An interaction between the microtubule-associated proteins (MAPs) and the outer surface of rat brain mitochondria has been demonstrated in vitro and in situ. One of the MAPs, MAP2, binds to specific high-affinity sites on the outer membrane. Upon binding, MAP2 is released from microtubules, and it induces a physical alteration in the outer membrane which is characterized by a tighter association of porin with the membrane. It is concluded that MAP2 either binds to porin or to a domain of the outer membrane which alters the membrane environment of porin. The possibility is raised that this domain participates in mitochondrial mobility in situ.
Lindén
M
M
Department of Biochemistry, University of Stockholm, Sweden.
Nelson
B D
BD
Loncar
D
D
Leterrier
J F
JF
D000818:Animals; D001665:Binding Sites; D001921:Brain / Q000378:metabolism; D003599:Cytoskeleton / Q000378:metabolism*; D006651:Histocytochemistry; D066298:In Vitro Techniques; D007425:Intracellular Membranes / Q000378:metabolism; D007473:Ion Channels / Q000378:metabolism; D008565:Membrane Proteins / Q000378:metabolism; D008869:Microtubule-Associated Proteins / Q000378:metabolism; D008870:Microtubules / Q000378:metabolism; D008928:Mitochondria / Q000378:metabolism* / Q000648:ultrastructure; D018272:Porins; D051381:Rats; D050994:Voltage-Dependent Anion Channels
D007473:Ion Channels; D008565:Membrane Proteins; D008869:Microtubule-Associated Proteins; D018272:Porins; D050994:Voltage-Dependent Anion Channels