Abstract:
:The regulation of glycogen metabolism is critical for the maintenance of glucose and energy homeostasis in mammals. Glycogen synthase, the enzyme responsible for glycogen production, is regulated by multisite phosphorylation in yeast and mammals. We have previously identified PAS kinase as a physiological regulator of glycogen synthase in Saccharomyces cerevisiae. We provide evidence here that PAS kinase is an important regulator of mammalian glycogen synthase. Glycogen synthase is efficiently phosphorylated by PAS kinase in vitro at Ser-640, a known regulatory phosphosite. Efficient phosphorylation requires a region of PAS kinase outside the catalytic domain. This region appears to mediate a direct interaction between glycogen synthase and PAS kinase, thereby targeting kinase activity to this substrate specifically. This interaction is regulated by the PAS kinase PAS domain, raising the possibility that this interaction (and phosphorylation event) is modulated by the cellular metabolic state. This mode of regulation provides a mechanism for metabolic status to impinge directly on the cellular decision of whether to store or use available energy.
journal_name
Proc Natl Acad Sci U S Aauthors
Wilson WA,Skurat AV,Probst B,de Paoli-Roach A,Roach PJ,Rutter Jdoi
10.1073/pnas.0508481102keywords:
subject
Has Abstractpub_date
2005-11-15 00:00:00pages
16596-601issue
46eissn
0027-8424issn
1091-6490pii
0508481102journal_volume
102pub_type
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