Disease relevance of PCL10

• We report that recombinant Pho85p and Pcl10p produced in Escherichia coli reconstitute an active Gsy2p kinase in vitro [1].

High impact information on PCL10

• We suggest a model for Pho85p function in the cell whereby cyclins like Pcl10p recruit Pho85p from a pool of monomers, both activating the kinase and targeting it to substrate [1].
• Gsy2p phosphorylation required Pcl10p, occurred at physiologically relevant sites, and resulted in inactivation of Gsy2p [1].
• Pcl10p is one of four Pcls with little sequence similarity to cyclins involved in cell cycle control [1].
• In contrast, deletion of PCL8 and PCL10 in the coq3 mutant background partially restores glycogen accumulation [2].

Associations of PCL10 with chemical compounds

• Glucose-6-P increased V(max)/K(m) by about 2-fold (state III), whereas phosphorylation by the cyclin-dependent protein kinase Pcl10p/Pho85p decreased V(max)/K(m) by approximately 30-fold (state I) [3].

Other interactions of PCL10

• In conjunction with Pcl8p and Pcl10p, Pho85p phosphorylates and regulates glycogen synthase [2].

Analytical, diagnostic and therapeutic context of PCL10

• Gel filtration of yeast cell lysates demonstrated that most Pho85p was present as a monomer, although a portion coeluted in high-molecular-weight fractions with Pcl10p and Gsy2p [1].

References