Yeast Pyruvate Dehydrogenase Complex Is Regulated by a Concerted Activity of Two Kinases and Two Phosphatases

Cornelia Czupalla,Uta Gey,Gerhard Rödel,Udo Krause-Buchholz,Bernard Hoflack

doi:10.1074/jbc.m708779200

Cornelia Czupalla, Uta Gey + Show 3 more

Open Access

https://doi.org/10.1074/jbc.m708779200

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Journal: Journal of Biological Chemistry	Publication Date: Apr 1, 2008
Citations: 81	License type: cc-by

Affiliation: TU Dresden

Abstract

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.

Highlights

Cies of the animalia, plants contain only one site, and a variable number is present in Fungi and Protista [10]
In analogy to the previously identified enzymes, we propose to name these new enzymes as pyruvate dehydrogenase complex (PDC) kinase II (Pkp2p) and PDC phosphatase II (Ppp2p)
The Protein Phosphatases Ppp2p and Yhr076wp and the Protein Kinase Pkp2p Are Localized in the Mitochondrial Compartment—We have previously identified two enzymes that phosphorylate (Pkp1p) and dephosphorylate (Ppp1p) Pda1p, thereby regulating the activity of PDC

Summary

Introduction

Cies of the animalia, plants contain only one site, and a variable number is present in Fungi and Protista [10]. We identified two enzymes that are involved in the phosphorylation (Pkp1p) and dephosphorylation (Ppp1p) of Pda1p, the ␣-subunit of the pyruvate dehydrogenase complex. 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.

Results

Conclusion