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Lookup NU author(s): Professor Loranne Agius
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Liver glycogen is synthesized after a meal in response to an increase in blood glucose concentration in the portal vein and endocrine and neuroendocrine signals, and is degraded to glucose between meals to maintain blood glucose homeostasis. Glycogen degradation and synthesis during the diurnal cycle are mediated by changes in the activities of phosphorylase and glycogen synthase. Phosphorylase is regulated by phosphorylation of serine-14. Only the phosphorylated form of liver phosphorylase (GPa) is catalytically active. Interconversion between GPa and GPb (unphosphorylated) is dependent on the activities of phosphorylase kinase and of phosphorylase phosphatase. The latter comprises protein phosphatase-1 in conjunction with a glycogen-targeting protein (G-subunit) of the PPP1R3 family. At least two of six G-subunits (GL and PTG) expressed in liver are involved in GPa dephosphorylation. GPa to GPb interconversion is dependent on the conformational state of phosphorylase which can be relaxed (R) or tense (T) depending on the concentrations of allosteric effectors such as glucose, glucose 6-phosphate and adenine nucleotides and on the acetylation state of lysine residues. The G-subunit, GL, encoded by PPP1R3B gene is expressed at high levels in liver and can function as a phosphorylase phosphatase and a synthase phosphatase and has an allosteric binding site for GPa at the C-terminus which inhibits synthase phosphatase activity. GPa to GPb conversion is a major upstream event in the regulation of glycogen synthesis by glucose, its downstream metabolites and extracellular signals such as insulin and neurotransmitters. (C) 2015 Elsevier Ltd. All rights reserved.
Author(s): Agius L
Publication type: Review
Publication status: Published
Journal: Molecular Aspects of Medicine
Year: 2015
Volume: 46
Pages: 34-45
Print publication date: 01/12/2015
Online publication date: 28/10/2015
Acceptance date: 11/09/2015
ISSN (print): 0098-2997
ISSN (electronic): 1872-9452
Publisher: ELSEVIER SCIENCE BV
URL: http://dx.doi.org/10.1016/j.mam.2015.09.002
DOI: 10.1016/j.mam.2015.09.002
