NADH is specifically channeled through the mitochondrial porin channel in Saccharomyces cerevisiae.
In many kinds of permeabilized cells, the restriction of metabolite diffusion by a mitochondrial porin "closed state" has been shown to control the respiration rate. However, since in isolated mitochondria the porin appears to be always "open," the physiological relevance of a putative regulation via this channel status is now a subject of discussion. In Saccharomyces cerevisiae, in which some of the NADH dehydrogenase active sites are facing the intermembrane space, this regulatory mechanism might play an important role for the regulation of the cytosolic redox status. Using permeabilized spheroplasts from wild-type and porin-deficient mutant, we show that the NADH produced in the cytosol is channeled to the mitochondrial NADH dehydrogenases through a metabolic network involving the porin channel. Thus, the control exerted by the porin (i.e., "open" or "closed" state) seems to be determined through its participation or not in organized metabolic networks.
Avéret
N
N
Institut de Biochimie et Génétique Cellulaires du CNRS, Université Victor Segalen Bordeaux 2, 1 rue Camille Saint-Saëns, F-33077 Bordeaux cedex, France.
Aguilaniu
H
H
Bunoust
O
O
Gustafsson
L
L
Rigoulet
M
M
D003600:Cytosol / Q000378:metabolism; D004579:Electron Transport; D017136:Ion Transport; D007700:Kinetics; D009154:Mutation; D009243:NAD / Q000378:metabolism*; D009247:NADH, NADPH Oxidoreductases / Q000378:metabolism; D010539:Permeability; D018272:Porins / Q000235:genetics / Q000378:metabolism*; D012441:Saccharomyces cerevisiae / Q000235:genetics / Q000378:metabolism*; D029701:Saccharomyces cerevisiae Proteins / Q000235:genetics / Q000378:metabolism*; D013104:Spheroplasts / Q000378:metabolism; D050994:Voltage-Dependent Anion Channels
D018272:Porins; D029701:Saccharomyces cerevisiae Proteins; D050994:Voltage-Dependent Anion Channels; D009243:NAD; D009247:NADH, NADPH Oxidoreductases