The yeast Pho80-Pho85 cyclin-CDK complex has multiple substrates.

Abstract

The Pho85-Pho80 cyclin-CDK (cyclin-dependent protein kinase) complex of Saccharomyces cerevisiae functions as a key regulator of the phosphate-repressible acid phosphatase system. We have further characterized the Pho85-Pho80 kinase complex and identified the Pho80 cyclin subunit and the Pho81 CDK inhibitor as substrates of the Pho85 protein kinase. The phosphorylation sites within Pho80 have been identified at Ser234 and Ser267. Of the two sites, phosphorylation of Ser234 is required for Pho80 function, to form an active kinase complex and repress acid phosphatase expression. Evidence suggests that the activity of Pho81 is regulated by a post-translational modification and therefore that Pho85-mediated phosphorylation of Pho81 may alter its ability to function as a CDK inhibitor. Thus, the control of acid phosphatase expression involves the phosphorylation of several of the regulatory components of the system.