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There has been debate over the relative importance of allosteric compared with covalent control of the key biosynthetic enzyme, glycogen synthase, as well as the relative importance of glucose entry into cells compared with glycogen synthase regulation in determining glycogen accumulation. Significant new developments in eukaryotic glycogen metabolism over the last decade or so include: (i) three-dimensional structures of the biosynthetic enzymes glycogenin and glycogen synthase, with associated implications for mechanism and control; (ii) analyses of several genetically engineered mice with altered glycogen metabolism that shed light on the mechanism of control; (iii) greater appreciation of the spatial aspects of glycogen metabolism, including more focus on the lysosomal degradation of glycogen; and (iv) glycogen phosphorylation and advances in the study of Lafora disease, which is emerging as a glycogen storage disease.<\/jats:p>","DOI":"10.1042\/bj20111416","type":"journal-article","created":{"date-parts":[[2012,1,16]],"date-time":"2012-01-16T15:53:29Z","timestamp":1326729209000},"page":"763-787","update-policy":"https:\/\/doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":659,"title":["Glycogen and its metabolism: some new developments and old themes"],"prefix":"10.1042","volume":"441","author":[{"given":"Peter\u00a0J.","family":"Roach","sequence":"first","affiliation":[{"name":"Department of Biochemistry and Molecular Biology, Indiana University School of Medicine, Indianapolis, IN 46202, U.S.A."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Anna\u00a0A.","family":"Depaoli-Roach","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Molecular Biology, Indiana University School of Medicine, Indianapolis, IN 46202, U.S.A."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Thomas\u00a0D.","family":"Hurley","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Molecular Biology, Indiana University School of Medicine, Indianapolis, IN 46202, U.S.A."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Vincent\u00a0S.","family":"Tagliabracci","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Molecular Biology, Indiana University School of Medicine, Indianapolis, IN 46202, U.S.A."}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"288","published-online":{"date-parts":[[2012,1,16]]},"reference":[{"key":"2021112215374273300_B1","first-page":"199","article-title":"The comparative biochemistry of glycogen and starch","volume-title":"Biology of Carbohydrates","author":"Preiss","year":"1981"},{"key":"2021112215374273300_B2","doi-asserted-by":"crossref","first-page":"349","DOI":"10.1016\/S0092-8674(00)80107-5","article-title":"From glycogen to amylopectin: a model for the biogenesis of the plant starch granule","volume":"86","author":"Ball","year":"1996","journal-title":"Cell"},{"key":"2021112215374273300_B3","doi-asserted-by":"crossref","first-page":"13","DOI":"10.1042\/BJ20061393","article-title":"The diurnal metabolism of leaf starch","volume":"401","author":"Zeeman","year":"2007","journal-title":"Biochem. J."},{"key":"2021112215374273300_B4","doi-asserted-by":"crossref","first-page":"1431","DOI":"10.1136\/bmj.1.5033.1431","article-title":"Claude Bernard and the discovery of glycogen: a century of retrospect","volume":"1","author":"Young","year":"1957","journal-title":"Br. Med. J."},{"key":"2021112215374273300_B5","doi-asserted-by":"crossref","first-page":"127","DOI":"10.1002\/dmr.5610030107","article-title":"Control of glycogen synthesis in health and disease","volume":"3","author":"Stalmans","year":"1987","journal-title":"Diabetes Metab. Rev."},{"key":"2021112215374273300_B6","doi-asserted-by":"crossref","first-page":"163","DOI":"10.4052\/tigg.8.183","article-title":"Glycogen in liver: characteristics and biosynthesis","volume":"8","author":"Gannon","year":"1996","journal-title":"Trends Glycosci. Glycotechnol."},{"key":"2021112215374273300_B7","doi-asserted-by":"crossref","first-page":"544","DOI":"10.1096\/fasebj.11.7.9212078","article-title":"The role of glucose 6-phosphate in the control of glycogen synthase","volume":"11","author":"Villar-Palasi","year":"1997","journal-title":"FASEB J."},{"key":"2021112215374273300_B8","doi-asserted-by":"crossref","first-page":"19","DOI":"10.1042\/bj3360019","article-title":"Specific features of glycogen metabolism in the liver","volume":"336","author":"Bollen","year":"1998","journal-title":"Biochem. J."},{"key":"2021112215374273300_B9","doi-asserted-by":"crossref","first-page":"139","DOI":"10.1515\/JBCPP.1998.9.2-4.139","article-title":"Novel aspects of the regulation of glycogen storage","volume":"9","author":"Roach","year":"1998","journal-title":"J. Basic Clin. Physiol. Pharmacol."},{"key":"2021112215374273300_B10","first-page":"349","article-title":"Biosynthesis of glycogen","volume-title":"Oligosaccharides in Chemistry and Biology: a Comprehensive Handbook","author":"Roach","year":"2000"},{"key":"2021112215374273300_B11","first-page":"609","article-title":"Regulation of glycogen metabolism. In Handbook of Physiology Section 7: The Endocrine System volume II.","volume-title":"The Endocrine Pancreas and Regulation of Metabolism","author":"Roach","year":"2001"},{"key":"2021112215374273300_B12","doi-asserted-by":"crossref","first-page":"101","DOI":"10.2174\/1566524024605761","article-title":"Glycogen and its metabolism","volume":"2","author":"Roach","year":"2002","journal-title":"Curr. Mol. 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Res."},{"key":"2021112215374273300_B28","doi-asserted-by":"crossref","first-page":"201","DOI":"10.1042\/bj1630201","article-title":"The molecular size and shape of liver glycogen","volume":"163","author":"Geddes","year":"1977","journal-title":"Biochem. J."},{"key":"2021112215374273300_B29","doi-asserted-by":"crossref","first-page":"1094","DOI":"10.1021\/bm100074p","article-title":"Nature of \u03b1 and \u03b2 particles in glycogen using molecular size distributions","volume":"11","author":"Sullivan","year":"2010","journal-title":"Biomacromolecules"},{"key":"2021112215374273300_B30","doi-asserted-by":"crossref","first-page":"238301","DOI":"10.1103\/PhysRevLett.98.238301","article-title":"Randomly hyperbranched polymers","volume":"98","author":"Konkolewicz","year":"2007","journal-title":"Phys. Rev. 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Sci."},{"key":"2021112215374273300_B40","doi-asserted-by":"crossref","first-page":"428","DOI":"10.1007\/s11910-007-0066-7","article-title":"Advances in Lafora progressive myoclonus epilepsy","volume":"7","author":"Delgado-Escueta","year":"2007","journal-title":"Curr. Neurol. Neurosci. Rep."},{"key":"2021112215374273300_B41","first-page":"83","article-title":"Lafora disease, seizures and sugars","volume":"26","author":"Andrade","year":"2007","journal-title":"Acta Myol."},{"key":"2021112215374273300_B42","doi-asserted-by":"crossref","first-page":"265","DOI":"10.1016\/S0165-0173(99)00003-X","article-title":"Corpora amylacea and the family of polyglucosan diseases","volume":"29","author":"Cavanagh","year":"1999","journal-title":"Brain Res. Rev."},{"key":"2021112215374273300_B43","first-page":"99","article-title":"Basophilic (mucoid) degeneration of myocardium: a disorder of glycogen metabolism","volume":"61","author":"Rosai","year":"1970","journal-title":"Am. J. 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Chem."},{"key":"2021112215374273300_B47","doi-asserted-by":"crossref","first-page":"6649","DOI":"10.1016\/S0021-9258(18)62583-9","article-title":"Control of phosphorylase activity in a muscle glycogen particle. II. Activation by calcium","volume":"245","author":"Heilmeyer","year":"1970","journal-title":"J. Biol. Chem."},{"key":"2021112215374273300_B48","doi-asserted-by":"crossref","first-page":"6657","DOI":"10.1016\/S0021-9258(18)62584-0","article-title":"Control of phosphorylase activity in a muscle glycogen particle. III. Regulation of phosphorylase phosphatase","volume":"245","author":"Haschke","year":"1970","journal-title":"J. Biol. 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Nutr."},{"key":"2021112215374273300_B67","doi-asserted-by":"crossref","first-page":"E141","DOI":"10.1152\/ajpendo.00712.2009","article-title":"Glucose transporters in the 21st Century","volume":"298","author":"Thorens","year":"2010","journal-title":"Am. J. Physiol. Endocrinol. Metab."},{"key":"2021112215374273300_B68","doi-asserted-by":"crossref","first-page":"117","DOI":"10.1111\/j.1432-1033.1975.tb03979.x","article-title":"A precursor of glycogen biosynthesis: \u03b1-1,4-glucan-protein","volume":"52","author":"Krisman","year":"1975","journal-title":"Eur. J. 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Chem."},{"key":"2021112215374273300_B98","doi-asserted-by":"crossref","first-page":"23799","DOI":"10.1016\/S0021-9258(20)80455-4","article-title":"Control of yeast glycogen synthase-2 by COOH-terminal phosphorylation","volume":"268","author":"Hardy","year":"1993","journal-title":"J. Biol. Chem."},{"key":"2021112215374273300_B99","doi-asserted-by":"crossref","first-page":"3289","DOI":"10.1128\/MCB.18.6.3289","article-title":"Cyclin partners determine Pho85 protein kinase substrate specificity in vitro and in vivo: control of glycogen biosynthesis by Pcl8 and Pcl10","volume":"18","author":"Huang","year":"1998","journal-title":"Mol. Cell. Biol."},{"key":"2021112215374273300_B100","doi-asserted-by":"crossref","first-page":"2961","DOI":"10.1096\/fasebj.4.12.2168324","article-title":"Control of glycogen synthase by hierarchal protein phosphorylation","volume":"4","author":"Roach","year":"1990","journal-title":"FASEB J."},{"key":"2021112215374273300_B101","doi-asserted-by":"crossref","first-page":"14139","DOI":"10.1016\/S0021-9258(18)98653-9","article-title":"Multisite and hierarchal protein phosphorylation","volume":"266","author":"Roach","year":"1991","journal-title":"J. Biol. Chem."},{"key":"2021112215374273300_B102","doi-asserted-by":"crossref","first-page":"219","DOI":"10.1006\/abbi.1993.1342","article-title":"Mechanisms of multisite phosphorylation and inactivation of rabbit muscle glycogen synthase","volume":"304","author":"Zhang","year":"1993","journal-title":"Arch. Biochem. 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J."},{"key":"2021112215374273300_B110","doi-asserted-by":"crossref","first-page":"9126","DOI":"10.1016\/S0021-9258(18)60501-0","article-title":"Synergistic phosphorylation of rabbit muscle glycogen synthase by cyclic AMP-dependent protein kinase and casein kinase I: implications for hormonal regulation of glycogen synthase","volume":"264","author":"Flotow","year":"1989","journal-title":"J. Biol. Chem."},{"key":"2021112215374273300_B111","doi-asserted-by":"crossref","first-page":"10022","DOI":"10.1074\/jbc.M207787200","article-title":"Insulin resistance of glycogen synthase mediated by O-linked N-acetylglucosamine","volume":"278","author":"Parker","year":"2003","journal-title":"J. Biol. Chem."},{"key":"2021112215374273300_B112","doi-asserted-by":"crossref","first-page":"1000","DOI":"10.1126\/science.1179689","article-title":"Regulation of cellular metabolism by protein lysine acetylation","volume":"327","author":"Zhao","year":"2010","journal-title":"Science"},{"key":"2021112215374273300_B113","doi-asserted-by":"crossref","first-page":"426","DOI":"10.1016\/S0968-0004(01)01836-9","article-title":"Combinatorial control of protein phosphatase-1","volume":"26","author":"Bollen","year":"2001","journal-title":"Trends Biochem. Sci."},{"key":"2021112215374273300_B114","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1152\/physrev.00013.2003","article-title":"Functional diversity of protein phosphatase-1, a cellular economizer and reset button","volume":"84","author":"Ceulemans","year":"2004","journal-title":"Physiol. Rev."},{"key":"2021112215374273300_B115","doi-asserted-by":"crossref","first-page":"15782","DOI":"10.1016\/S0021-9258(18)98477-2","article-title":"Molecular cloning and expression of the regulatory (RG1) subunit of the glycogen-associated protein phosphatase","volume":"266","author":"Tang","year":"1991","journal-title":"J. Biol. Chem."},{"key":"2021112215374273300_B116","doi-asserted-by":"crossref","first-page":"294","DOI":"10.1016\/0014-5793(95)01184-G","article-title":"Amino acid sequence and expression of the hepatic glycogen-binding (GL)-subunit of protein phosphatase-1","volume":"375","author":"Doherty","year":"1995","journal-title":"FEBS Lett."},{"key":"2021112215374273300_B117","doi-asserted-by":"crossref","first-page":"101","DOI":"10.1016\/0014-5793(95)00197-H","article-title":"Purification of the hepatic glycogen-associated form of protein phosphatase-1 by microcystin\u2013Sepharose affinity chromatography","volume":"362","author":"Moorhead","year":"1995","journal-title":"FEBS Lett."},{"key":"2021112215374273300_B118","doi-asserted-by":"crossref","first-page":"253","DOI":"10.1042\/bj3330253","article-title":"Loss of the hepatic glycogen-binding subunit (GL) of protein phosphatase 1 underlies deficient glycogen synthesis in insulin-dependent diabetic rats and in adrenalectomized starved rats","volume":"333","author":"Doherty","year":"1998","journal-title":"Biochem. J."},{"key":"2021112215374273300_B119","doi-asserted-by":"crossref","first-page":"339","DOI":"10.1016\/S0014-5793(96)01357-9","article-title":"Amino acid sequence of a novel protein phosphatase 1 binding protein (R5) which is related to the liver- and muscle-specific glycogen binding subunits of protein phosphatase 1","volume":"399","author":"Doherty","year":"1996","journal-title":"FEBS Lett."},{"key":"2021112215374273300_B120","doi-asserted-by":"crossref","first-page":"1475","DOI":"10.1126\/science.275.5305.1475","article-title":"PTG, a protein phosphatase 1-binding protein with a role in glycogen metabolism","volume":"275","author":"Printen","year":"1997","journal-title":"Science"},{"key":"2021112215374273300_B121","doi-asserted-by":"crossref","first-page":"699","DOI":"10.1042\/bj3360699","article-title":"Identification of the separate domains in the hepatic glycogen-targeting subunit of protein phosphatase 1 that interact with phosphorylase a, glycogen and protein phosphatase 1","volume":"336","author":"Armstrong","year":"1998","journal-title":"Biochem. 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Natl. Acad. Sci. U.S.A."},{"key":"2021112215374273300_B126","doi-asserted-by":"crossref","first-page":"3196","DOI":"10.1038\/sj.emboj.7600324","article-title":"Crystal structure of glycogen synthase: homologous enzymes catalyze glycogen synthesis and degradation","volume":"23","author":"Buschiazzo","year":"2004","journal-title":"EMBO J."},{"key":"2021112215374273300_B127","doi-asserted-by":"crossref","first-page":"2923","DOI":"10.1074\/jbc.M507394200","article-title":"Crystal structure of an archaeal glycogen synthase: insights into oligomerization and substrate binding of eukaryotic glycogen synthases","volume":"281","author":"Horcajada","year":"2006","journal-title":"J. Biol. Chem."},{"key":"2021112215374273300_B128","doi-asserted-by":"crossref","first-page":"17796","DOI":"10.1074\/jbc.M809804200","article-title":"The crystal structures of the open and catalytically competent closed conformation of Escherichia coli glycogen synthase","volume":"284","author":"Sheng","year":"2009","journal-title":"J. Biol. Chem."},{"key":"2021112215374273300_B129","doi-asserted-by":"crossref","first-page":"253","DOI":"10.1006\/jmbi.1993.1380","article-title":"Crystallographic binding studies on the allosteric inhibitor glucose-6-phosphate to T state glycogen phosphorylase b","volume":"232","author":"Johnson","year":"1993","journal-title":"J. Mol. Biol."},{"key":"2021112215374273300_B130","doi-asserted-by":"crossref","first-page":"27753","DOI":"10.1016\/S0021-9258(19)65048-9","article-title":"Regulation of glycogen synthase: identification of residues involved in regulation by the allosteric ligand glucose-6-P and by phosphorylation","volume":"275","author":"Pederson","year":"2000","journal-title":"J. Biol. Chem."},{"key":"2021112215374273300_B131","doi-asserted-by":"crossref","first-page":"2409","DOI":"10.1016\/S0021-9258(19)39810-2","article-title":"Glycogen phosphorylase: the structural basis of the allosteric response and comparison with other allosteric proteins","volume":"265","author":"Johnson","year":"1990","journal-title":"J. Biol. Chem."},{"key":"2021112215374273300_B132","doi-asserted-by":"crossref","first-page":"18505","DOI":"10.1074\/jbc.M111.236109","article-title":"Processivity and subcellular localization of glycogen synthase depend on a non-catalytic high affinity glycogen-binding site","volume":"286","author":"D\u00edaz","year":"2011","journal-title":"J. Biol. Chem."},{"key":"2021112215374273300_B133","doi-asserted-by":"crossref","first-page":"33999","DOI":"10.1074\/jbc.M111.264531","article-title":"Multiple glycogen binding sites in eukaryotic glycogen synthase are required for high catalytic efficiency toward glycogen","volume":"286","author":"Baskaran","year":"2011","journal-title":"J. Biol. Chem."},{"key":"2021112215374273300_B134","doi-asserted-by":"crossref","first-page":"33614","DOI":"10.1074\/jbc.M005358200","article-title":"Identification of two essential glutamic acid residues in glycogen synthase","volume":"275","author":"Cid","year":"2000","journal-title":"J. Biol. Chem."},{"key":"2021112215374273300_B135","doi-asserted-by":"crossref","first-page":"426","DOI":"10.1042\/bj0510426","article-title":"Studies on uridine-diphosphate-glucose","volume":"51","author":"Paladini","year":"1952","journal-title":"Biochem. J."},{"key":"2021112215374273300_B136","doi-asserted-by":"crossref","first-page":"284","DOI":"10.1016\/j.ymgme.2005.10.006","article-title":"Hepatic glycogen synthase deficiency: an infrequently recognized cause of ketotic hypoglycemia","volume":"87","author":"Weinstein","year":"2006","journal-title":"Mol. Genet. Metab."},{"key":"2021112215374273300_B137","doi-asserted-by":"crossref","first-page":"507","DOI":"10.1172\/JCI2890","article-title":"Mutations in the liver glycogen synthase gene in children with hypoglycemia due to glycogen storage disease type\u00a00","volume":"102","author":"Orho","year":"1998","journal-title":"J. Clin. Invest."},{"key":"2021112215374273300_B138","doi-asserted-by":"crossref","first-page":"12851","DOI":"10.1074\/jbc.M110.106534","article-title":"Impaired glucose tolerance and predisposition to the fasted state in liver glycogen synthase knock-out mice","volume":"285","author":"Irimia","year":"2010","journal-title":"J. Biol. Chem."},{"key":"2021112215374273300_B139","doi-asserted-by":"crossref","first-page":"1507","DOI":"10.1056\/NEJMoa066691","article-title":"Cardiomyopathy and exercise intolerance in muscle glycogen storage disease 0","volume":"357","author":"Kollberg","year":"2007","journal-title":"N. Engl. J. Med."},{"key":"2021112215374273300_B140","doi-asserted-by":"crossref","first-page":"378","DOI":"10.1016\/j.ymgme.2009.07.012","article-title":"Identification of a novel mutation in GYS1 (muscle-specific glycogen synthase) resulting in sudden cardiac death, that is diagnosable from skin fibroblasts","volume":"98","author":"Cameron","year":"2009","journal-title":"Mol. Genet. 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Med."},{"key":"2021112215374273300_B144","doi-asserted-by":"crossref","first-page":"1149","DOI":"10.1042\/bst0071149","article-title":"Molecular democracy: who shares the controls?","volume":"7","author":"Kacser","year":"1979","journal-title":"Biochem. Soc. Trans."},{"key":"2021112215374273300_B145","doi-asserted-by":"crossref","first-page":"171","DOI":"10.1016\/0006-3002(60)90142-6","article-title":"Insulin-mediated effect on the activity of UDPG-glycogen transglucosylase of muscle","volume":"39","author":"Villar-Palasi","year":"1960","journal-title":"Biochim. Biophys. Acta"},{"key":"2021112215374273300_B146","doi-asserted-by":"crossref","first-page":"16113","DOI":"10.1016\/S0021-9258(19)85395-4","article-title":"Evidence from transgenic mice that glucose transport is rate-limiting for glycogen deposition and glycolysis in skeletal muscle","volume":"268","author":"Ren","year":"1993","journal-title":"J. Biol. Chem."},{"key":"2021112215374273300_B147","doi-asserted-by":"crossref","first-page":"1679","DOI":"10.1016\/S0021-9258(18)85410-2","article-title":"Skeletal muscle glucose transport and metabolism are enhanced in transgenic mice overexpressing the Glut4 glucose transporter","volume":"270","author":"Hansen","year":"1995","journal-title":"J. Biol. Chem."},{"key":"2021112215374273300_B148","doi-asserted-by":"crossref","first-page":"9713","DOI":"10.1128\/MCB.25.21.9713-9723.2005","article-title":"Muscle-specific deletion of the Glut4 glucose transporter alters multiple regulatory steps in glycogen metabolism","volume":"25","author":"Kim","year":"2005","journal-title":"Mol. Cell. 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U.S.A."},{"key":"2021112215374273300_B151","doi-asserted-by":"crossref","first-page":"39959","DOI":"10.1074\/jbc.M105518200","article-title":"The muscle specific protein phosphatase PP1G\/RGL(GM) is essential for activation of glycogen synthase by exercise","volume":"276","author":"Aschenbach","year":"2001","journal-title":"J. Biol. Chem."},{"key":"2021112215374273300_B152","doi-asserted-by":"crossref","first-page":"2683","DOI":"10.1128\/MCB.21.8.2683-2694.2001","article-title":"Insulin control of glycogen metabolism in knockout mice lacking the muscle-specific protein phosphatase PP1G\/RGL","volume":"21","author":"Suzuki","year":"2001","journal-title":"Mol. Cell. Biol."},{"key":"2021112215374273300_B153","doi-asserted-by":"crossref","first-page":"596","DOI":"10.2337\/diabetes.52.3.596","article-title":"Disruption of the striated muscle glycogen targeting subunit PPP1R3A of protein phosphatase 1 leads to increased weight gain, fat deposition, and development of insulin resistance","volume":"52","author":"Delibegovic","year":"2003","journal-title":"Diabetes"},{"key":"2021112215374273300_B154","doi-asserted-by":"crossref","first-page":"e27","DOI":"10.1371\/journal.pmed.0050027","article-title":"A prevalent variant in PPP1R3A impairs glycogen synthesis and reduces muscle glycogen content in humans and mice","volume":"5","author":"Savage","year":"2008","journal-title":"PLoS Med."},{"key":"2021112215374273300_B155","first-page":"A62","article-title":"Enhanced insulin sensitivity and energy expenditure in PPP1R3C (PTG) deleted mice","volume":"56","author":"Zhai","year":"2007","journal-title":"Diabetes"},{"key":"2021112215374273300_B156","doi-asserted-by":"crossref","first-page":"1423","DOI":"10.1172\/JCI17975","article-title":"PTG gene deletion causes impaired glycogen synthesis and developmental insulin resistance","volume":"111","author":"Crosson","year":"2003","journal-title":"J. Clin. Invest."},{"key":"2021112215374273300_B157","doi-asserted-by":"crossref","first-page":"7491","DOI":"10.1073\/pnas.93.15.7491","article-title":"Enzymatic phosphorylation of muscle glycogen synthase: a mechanism for maintenance of metabolic homeostasis","volume":"93","author":"Shulman","year":"1996","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"2021112215374273300_B158","doi-asserted-by":"crossref","first-page":"8535","DOI":"10.1073\/pnas.92.19.8535","article-title":"In vivo regulation of muscle glycogen synthase and the control of glycogen synthesis","volume":"92","author":"Shulman","year":"1995","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"2021112215374273300_B159","doi-asserted-by":"crossref","first-page":"E598","DOI":"10.1152\/ajpendo.2001.280.4.E598","article-title":"Flux control in the rat gastrocnemius glycogen synthesis pathway by in vivo 13C\/31P NMR spectroscopy","volume":"280","author":"Chase","year":"2001","journal-title":"Am. J. Physiol. 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Physiol."},{"key":"2021112215374273300_B163","doi-asserted-by":"crossref","first-page":"304","DOI":"10.1111\/j.1753-4887.2000.tb01825.x","article-title":"Is in vivo nuclear magnetic resonance spectroscopy currently a quantitative method for whole-body carbohydrate metabolism?","volume":"58","author":"Murphy","year":"2000","journal-title":"Nutr. Rev."},{"key":"2021112215374273300_B164","doi-asserted-by":"crossref","first-page":"541","DOI":"10.2337\/diab.46.4.541","article-title":"New insights into the role and mechanism of glycogen synthase activation by insulin","volume":"46","author":"Lawrence","year":"1997","journal-title":"Diabetes"},{"key":"2021112215374273300_B165","doi-asserted-by":"crossref","first-page":"443","DOI":"10.1111\/j.1432-1033.1981.tb05628.x","article-title":"Purification of glycogen synthase kinase 3 from rabbit skeletal muscle: copurification with the activating factor (FA) of the (Mg-ATP) dependent protein phosphatase","volume":"119","author":"Hemmings","year":"1981","journal-title":"Eur. J. Biochem."},{"key":"2021112215374273300_B166","doi-asserted-by":"crossref","first-page":"R236","DOI":"10.1016\/S0960-9822(02)00777-7","article-title":"The insulin signalling pathway","volume":"12","author":"Lizcano","year":"2002","journal-title":"Curr. Biol."},{"key":"2021112215374273300_B167","doi-asserted-by":"crossref","first-page":"150","DOI":"10.1016\/j.ceb.2005.02.010","article-title":"Recent advances in the protein kinase B signaling pathway","volume":"17","author":"Woodgett","year":"2005","journal-title":"Curr. Opin. Cell. Biol."},{"key":"2021112215374273300_B168","doi-asserted-by":"crossref","first-page":"1322","DOI":"10.1016\/j.metabol.2004.05.008","article-title":"Development of glucose intolerance in male transgenic mice overexpressing human glycogen synthase kinase-3\u03b2 on a muscle-specific promoter","volume":"53","author":"Pearce","year":"2004","journal-title":"Metabolism"},{"key":"2021112215374273300_B169","doi-asserted-by":"crossref","first-page":"10710","DOI":"10.1016\/S0021-9258(17)44514-5","article-title":"Hormonal control of glycogen synthase in rat hemidiaphragms: effects of insulin and epinephrine on the distribution of phosphate between two cyanogen bromide fragments","volume":"258","author":"Lawrence","year":"1983","journal-title":"J. Biol. Chem."},{"key":"2021112215374273300_B170","doi-asserted-by":"crossref","first-page":"227","DOI":"10.1111\/j.1432-1033.1983.tb07140.x","article-title":"Glycogen synthase from rabbit skeletal muscle: effect of insulin on the state of phosphorylation of the seven phosphoserine residues in vivo","volume":"130","author":"Parker","year":"1983","journal-title":"Eur. J. Biochem."},{"key":"2021112215374273300_B171","doi-asserted-by":"crossref","first-page":"2490","DOI":"10.1074\/jbc.M301769200","article-title":"Phosphorylation of Ser640 in muscle glycogen synthase by DYRK family protein kinases","volume":"279","author":"Skurat","year":"2004","journal-title":"J. Biol. Chem."},{"key":"2021112215374273300_B172","doi-asserted-by":"crossref","first-page":"133","DOI":"10.1042\/bj20031559","article-title":"Identification of glycogen synthase as a new substrate for stress-activated protein kinase 2b\/p38\u03b2","volume":"379","author":"Kuma","year":"2004","journal-title":"Biochem. J."},{"key":"2021112215374273300_B173","doi-asserted-by":"crossref","first-page":"16596","DOI":"10.1073\/pnas.0508481102","article-title":"Control of mammalian glycogen synthase by PAS kinase","volume":"102","author":"Wilson","year":"2006","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"2021112215374273300_B174","doi-asserted-by":"crossref","first-page":"1571","DOI":"10.1038\/sj.emboj.7600633","article-title":"Role that phosphorylation of GSK3 plays in insulin and Wnt signalling defined by knockin analysis","volume":"24","author":"McManus","year":"2005","journal-title":"EMBO J."},{"key":"2021112215374273300_B175","doi-asserted-by":"crossref","first-page":"309","DOI":"10.1046\/j.1365-201X.2003.01165.x","article-title":"Regulation of glycogen synthase in skeletal muscle during exercise","volume":"178","author":"Nielsen","year":"2003","journal-title":"Acta Physiol. Scand."},{"key":"2021112215374273300_B176","doi-asserted-by":"crossref","first-page":"233","DOI":"10.1079\/PNS2004348","article-title":"Regulation of glycogen synthase activity and phosphorylation by exercise","volume":"63","author":"Nielsen","year":"2004","journal-title":"Proc. Nutr. Soc."},{"key":"2021112215374273300_B177","doi-asserted-by":"crossref","first-page":"457","DOI":"10.1073\/pnas.98.2.457","article-title":"The \u201cglycogen shunt\u201d in exercising muscle: a role for glycogen in muscle energetics and fatigue","volume":"98","author":"Shulman","year":"2001","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"2021112215374273300_B178","doi-asserted-by":"crossref","first-page":"1257","DOI":"10.1172\/JCI7961","article-title":"Exercise modulates postreceptor insulin signaling and glucose transport in muscle-specific insulin receptor knockout mice","volume":"104","author":"Wojtaszewski","year":"1999","journal-title":"J. Clin. Invest."},{"key":"2021112215374273300_B179","doi-asserted-by":"crossref","first-page":"701","DOI":"10.1111\/j.1432-1033.1989.tb15263.x","article-title":"Regulation of protein phosphatase-1G from rabbit skeletal muscle. 1. Phosphorylation by cAMP-dependent protein kinase at site 2 releases catalytic subunit from the glycogen-bound holoenzyme","volume":"186","author":"Hubbard","year":"1989","journal-title":"Eur. J. Biochem."},{"key":"2021112215374273300_B180","doi-asserted-by":"crossref","first-page":"E1622","DOI":"10.1152\/ajpendo.00113.2007","article-title":"Glycogen content and contraction regulate glycogen synthase phosphorylation and affinity for UDP-glucose in rat skeletal muscles","volume":"293","author":"Lai","year":"2007","journal-title":"Am. J. Physiol. Endocrinol. 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Chem."},{"key":"2021112215374273300_B188","doi-asserted-by":"crossref","first-page":"99","DOI":"10.1111\/j.1748-1716.2009.01975.x","article-title":"AMP-activated protein kinase: a sensor of glycogen as well as AMP and ATP?","volume":"196","author":"McBride","year":"2009","journal-title":"Acta Physiol."},{"key":"2021112215374273300_B189","doi-asserted-by":"crossref","first-page":"1248","DOI":"10.1126\/science.288.5469.1248","article-title":"A mutation in PRKAG3 associated with excess glycogen content in pig skeletal muscle","volume":"288","author":"Milan","year":"2000","journal-title":"Science"},{"key":"2021112215374273300_B190","doi-asserted-by":"crossref","first-page":"474","DOI":"10.1161\/01.RES.0000258446.23525.37","article-title":"AMP-activated protein kinase in the heart: role during health and disease","volume":"100","author":"Arad","year":"2007","journal-title":"Circ. Res."},{"key":"2021112215374273300_B191","doi-asserted-by":"crossref","first-page":"25372","DOI":"10.1074\/jbc.M110.148668","article-title":"Genetic depletion of the malin E3 ubiquitin ligase in mice leads to Lafora bodies and the accumulation of insoluble laforin","volume":"285","author":"DePaoli-Roach","year":"2010","journal-title":"J. Biol. Chem."},{"key":"2021112215374273300_B192","doi-asserted-by":"crossref","first-page":"13764","DOI":"10.1074\/jbc.M312335200","article-title":"Glycogen synthase sensitivity to glucose-6-P is important for controlling glycogen accumulation in Saccharomyces cerevisiae","volume":"279","author":"Pederson","year":"2004","journal-title":"J. Biol. Chem."},{"key":"2021112215374273300_B193","doi-asserted-by":"crossref","first-page":"456","DOI":"10.1016\/j.cmet.2010.10.006","article-title":"Allosteric regulation of glycogen synthase controls glycogen synthesis in muscle","volume":"12","author":"Bouskila","year":"2010","journal-title":"Cell Metab."},{"key":"2021112215374273300_B194","doi-asserted-by":"crossref","first-page":"286","DOI":"10.1006\/abbi.2001.2623","article-title":"Mutations of muscle glycogen synthase that disable activation by glucose 6-phosphate","volume":"397","author":"Hanashiro","year":"2002","journal-title":"Arch. Biochem. Biophys."},{"key":"2021112215374273300_B195","doi-asserted-by":"crossref","first-page":"766","DOI":"10.2337\/db10-1148","article-title":"Molecular mechanism by which AMP-activated protein kinase activation promotes glycogen accumulation in muscle","volume":"60","author":"Hunter","year":"2011","journal-title":"Diabetes"},{"key":"2021112215374273300_B196","doi-asserted-by":"crossref","first-page":"381","DOI":"10.1111\/j.1748-1716.1989.tb08591.x","article-title":"Topographical localization of muscle glycogen: an ultrahistochemical study in the human vastus lateralis","volume":"135","author":"Friden","year":"1989","journal-title":"Acta Physiol. Scand."},{"key":"2021112215374273300_B197","doi-asserted-by":"crossref","first-page":"617","DOI":"10.1113\/jphysiol.2006.122457","article-title":"Quantitative assessment of human muscle glycogen granules size and number in subcellular locations during recovery from prolonged exercise","volume":"580","author":"Marchand","year":"2007","journal-title":"J. Physiol."},{"key":"2021112215374273300_B198","doi-asserted-by":"crossref","first-page":"3679","DOI":"10.1113\/jphysiol.2009.174862","article-title":"Distinct effects of subcellular glycogen localization on tetanic relaxation time and endurance in mechanically skinned rat skeletal muscle fibres","volume":"587","author":"Nielsen","year":"2009","journal-title":"J. Physiol."},{"key":"2021112215374273300_B199","doi-asserted-by":"crossref","first-page":"2627","DOI":"10.1021\/bi00764a013","article-title":"Metabolic profiles of three fiber types\u00a0of skeletal muscle in guinea pigs and rabbits","volume":"11","author":"Peter","year":"1972","journal-title":"Biochemistry"},{"key":"2021112215374273300_B200","doi-asserted-by":"crossref","first-page":"179","DOI":"10.1146\/annurev.nu.16.070196.001143","article-title":"Zonation of parenchymal and nonparenchymal metabolism in liver","volume":"16","author":"Jungermann","year":"1996","journal-title":"Annu. Rev. Nutr."},{"key":"2021112215374273300_B201","doi-asserted-by":"crossref","first-page":"277","DOI":"10.1016\/0014-5793(87)80940-7","article-title":"Glycogen synthesis from pyruvate in the periportal and from glucose in the perivenous zone in perfused livers from fasted rats","volume":"221","author":"Bartels","year":"1987","journal-title":"FEBS Lett."},{"key":"2021112215374273300_B202","doi-asserted-by":"crossref","first-page":"136","DOI":"10.1042\/bst0250136","article-title":"The regulatory protein of glucokinase","volume":"25","author":"van Schaftingen","year":"1997","journal-title":"Biochem. Soc. Trans."},{"key":"2021112215374273300_B203","doi-asserted-by":"crossref","first-page":"167","DOI":"10.1146\/annurev.bi.45.070176.001123","article-title":"The control of glycogen metabolism in the liver","volume":"45","author":"Hers","year":"1976","journal-title":"Annu. Rev. Biochem."},{"key":"2021112215374273300_B204","doi-asserted-by":"crossref","first-page":"4749","DOI":"10.1016\/j.febslet.2007.08.073","article-title":"The hepatic PP1 glycogen-targeting subunit interaction with phosphorylase a can be blocked by C-terminal tyrosine deletion or an indole drug","volume":"581","author":"Kelsall","year":"2007","journal-title":"FEBS Lett."},{"key":"2021112215374273300_B205","doi-asserted-by":"crossref","first-page":"1123","DOI":"10.1016\/j.cellsig.2009.03.001","article-title":"Disruption of the allosteric phosphorylase a regulation of the hepatic glycogen-targeted protein phosphatase 1 improves glucose tolerance in vivo","volume":"21","author":"Kelsall","year":"2009","journal-title":"Cell. 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Microbiol."},{"key":"2021112215374273300_B209","doi-asserted-by":"crossref","first-page":"494","DOI":"10.1210\/en.2004-1022","article-title":"Spatial reorganization of glycogen synthase upon activation in 3T3-L1 adipocytes","volume":"146","author":"Ou","year":"2005","journal-title":"Endocrinology"},{"key":"2021112215374273300_B210","doi-asserted-by":"crossref","first-page":"23165","DOI":"10.1074\/jbc.M502713200","article-title":"Phosphorylation-dependent translocation of glycogen synthase to a novel structure during glycogen resynthesis","volume":"280","author":"Prats","year":"2005","journal-title":"J. Biol. Chem."},{"key":"2021112215374273300_B211","doi-asserted-by":"crossref","first-page":"15692","DOI":"10.1074\/jbc.M900845200","article-title":"Dual regulation of muscle glycogen synthase during exercise by activation and compartmentalization","volume":"284","author":"Prats","year":"2009","journal-title":"J. Biol. Chem."},{"key":"2021112215374273300_B212","doi-asserted-by":"crossref","first-page":"318","DOI":"10.4161\/auto.2984","article-title":"Autophagy and lysosomes in Pompe disease","volume":"2","author":"Fukuda","year":"2006","journal-title":"Autophagy"},{"key":"2021112215374273300_B213","doi-asserted-by":"crossref","first-page":"339","DOI":"10.1016\/0008-6215(92)85083-C","article-title":"Molecular and metabolic aspects of lysosomal glycogen","volume":"227","author":"Geddes","year":"1992","journal-title":"Carbohydr. Res."},{"key":"2021112215374273300_B214","first-page":"1","article-title":"An overview of the molecular mechanism of autophagy","volume":"335","author":"Yang","year":"2009","journal-title":"Curr. Top. Microbiol. Immunol."},{"key":"2021112215374273300_B215","doi-asserted-by":"crossref","first-page":"124","DOI":"10.1016\/j.ceb.2009.11.014","article-title":"Mammalian autophagy: core molecular machinery and signaling regulation","volume":"22","author":"Yang","year":"2010","journal-title":"Curr. Opin. Cell Biol."},{"key":"2021112215374273300_B216","doi-asserted-by":"crossref","first-page":"458","DOI":"10.1038\/nrm2708","article-title":"Dynamics and diversity in autophagy mechanisms: lessons from yeast","volume":"10","author":"Nakatogawa","year":"2009","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"2021112215374273300_B217","first-page":"431","article-title":"Selective autophagy regulates various cellular functions","volume":"32","author":"Komatsu","year":"2010","journal-title":"Genes Cells"},{"key":"2021112215374273300_B218","doi-asserted-by":"crossref","first-page":"279","DOI":"10.4161\/auto.7.3.14487","article-title":"Selective autophagy mediated by autophagic adapter proteins","volume":"7","author":"Johansen","year":"2011","journal-title":"Autophagy"},{"key":"2021112215374273300_B219","doi-asserted-by":"crossref","first-page":"10","DOI":"10.1002\/jemt.20046","article-title":"Glycogen autophagy","volume":"64","author":"Kotoulas","year":"2004","journal-title":"Microsc. Res. Tech."},{"key":"2021112215374273300_B220","doi-asserted-by":"crossref","first-page":"87","DOI":"10.1016\/B978-1-4832-2754-2.50009-8","article-title":"Physiological aspects of carbohydrate metabolism in the foetus and newborn","volume-title":"Carbohydrate Metabolism and Its Disorders","author":"Dawes","year":"1968"},{"key":"2021112215374273300_B221","first-page":"45","article-title":"Role of autophagy in the pathogenesis of Pompe disease","volume":"26","author":"Raben","year":"2007","journal-title":"Acta Myol."},{"key":"2021112215374273300_B222","doi-asserted-by":"crossref","first-page":"3897","DOI":"10.1093\/hmg\/ddn292","article-title":"Suppression of autophagy in skeletal muscle uncovers the accumulation of ubiquitinated proteins and their potential role in muscle damage in Pompe disease","volume":"17","author":"Raben","year":"2008","journal-title":"Hum. Mol. 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Chem."},{"key":"2021112215374273300_B227","doi-asserted-by":"crossref","first-page":"456","DOI":"10.1126\/science.1196371","article-title":"Phosphorylation of ULK1 (hATG1) by AMP-activated protein kinase connects energy sensing to mitophagy","volume":"331","author":"Egan","year":"2011","journal-title":"Science"},{"key":"2021112215374273300_B228","doi-asserted-by":"crossref","first-page":"132","DOI":"10.1038\/ncb2152","article-title":"AMPK and mTOR regulate autophagy through direct phosphorylation of Ulk1","volume":"13","author":"Kim","year":"2011","journal-title":"Nat. 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