Yeast pyruvate dehydrogenase complex is regulated by a concerted activity of two kinases and two phosphatases.
The activity of yeast pyruvate dehydrogenase complex is regulated by reversible phosphorylation. Recently we identified two enzymes that are involved in the phosphorylation (Pkp1p) and dephosphorylation (Ppp1p) of Pda1p, the alpha-subunit of the pyruvate dehydrogenase complex. Here we provide evidence that two additional mitochondrial proteins, Pkp2p (Ygl059wp) and Ppp2p (Ycr079wp), are engaged in the regulation of this complex by affecting the phosphorylation state of Pda1p. Our data indicate complementary activities of the kinases and a redundant function for the phosphatases. Both proteins are associated with the complex. We propose a model for the role of the regulatory enzymes and the phosphorylation state of Pda1p in the assembly process of the pyruvate dehydrogenase complex.
Gey
Uta
U
Institute of Genetics, Dresden University of Technology, 01062 Dresden, Germany.
Czupalla
Cornelia
C
Hoflack
Bernard
B
Rödel
Gerhard
G
Krause-Buchholz
Udo
U
D008954:Models, Biological; D010749:Phosphoprotein Phosphatases / Q000235:genetics / Q000378:metabolism*; D010766:Phosphorylation; D011494:Protein Kinases / Q000235:genetics / Q000378:metabolism*; D011768:Pyruvate Dehydrogenase Complex / Q000235:genetics / Q000378:metabolism*; D012441:Saccharomyces cerevisiae / Q000201:enzymology* / Q000235:genetics; D029701:Saccharomyces cerevisiae Proteins / Q000235:genetics / Q000378:metabolism*
D011768:Pyruvate Dehydrogenase Complex; D029701:Saccharomyces cerevisiae Proteins; D011494:Protein Kinases; C518822:PTC6 protein, S cerevisiae; D010749:Phosphoprotein Phosphatases