Alexander V Skurat

Summary

Affiliation: Indiana University
Country: USA

Publications

  1. ncbi request reprint Glycogen synthase sensitivity to insulin and glucose-6-phosphate is mediated by both NH2- and COOH-terminal phosphorylation sites
    A V Skurat
    Department of Biochemistry and Molecular Biology, Indiana University School of Medicine, Indianapolis 46202 USA
    Diabetes 49:1096-100. 2000
  2. ncbi request reprint Phosphorylation of Ser640 in muscle glycogen synthase by DYRK family protein kinases
    Alexander V Skurat
    Department of Biochemistry and Molecular Biology, Indiana University School of Medicine, Indianapolis, Indiana 46202, USA
    J Biol Chem 279:2490-8. 2004
  3. pmc Interaction between glycogenin and glycogen synthase
    Alexander V Skurat
    Department of Biochemistry and Molecular Biology, Indiana University School of Medicine, Indianapolis, IN 46202 5122, USA
    Arch Biochem Biophys 456:93-7. 2006
  4. pmc Laforin is a glycogen phosphatase, deficiency of which leads to elevated phosphorylation of glycogen in vivo
    Vincent S Tagliabracci
    Department of Biochemistry and Molecular Biology, Indiana University School of Medicine, Indianapolis, IN 46202, USA
    Proc Natl Acad Sci U S A 104:19262-6. 2007
  5. ncbi request reprint GNIP, a novel protein that binds and activates glycogenin, the self-glucosylating initiator of glycogen biosynthesis
    Alexander V Skurat
    Department of Biochemistry and Molecular Biology and Center for Diabetes Research, Indiana University School of Medicine, Indianapolis, Indiana 46202, USA
    J Biol Chem 277:19331-8. 2002
  6. ncbi request reprint Structure-function analysis of GNIP, the glycogenin-interacting protein
    Lanmin Zhai
    Department of Biochemistry and Molecular Biology, Center for Diabetes Research, Indiana University School of Medicine, 635 Barnhill Drive, Indianapolis, IN 46202 5122, USA
    Arch Biochem Biophys 421:236-42. 2004
  7. pmc Glycogen metabolism in tissues from a mouse model of Lafora disease
    Wei Wang
    Department of Biochemistry and Molecular Biology, Indiana University School of Medicine, Indianapolis, IN 46202 5122, USA
    Arch Biochem Biophys 457:264-9. 2007
  8. pmc Starch binding domain-containing protein 1/genethonin 1 is a novel participant in glycogen metabolism
    Sixin Jiang
    Department of Biochemistry and Molecular Biology, Indiana University School of Medicine, Indianapolis, Indiana 46202, USA
    J Biol Chem 285:34960-71. 2010
  9. ncbi request reprint Overexpression of glycogen synthase in mouse muscle results in less branched glycogen
    Bartholomew A Pederson
    Department of Biochemistry and Molecular Biology, Indiana University School of Medicine, and Indiana University Center for Diabetes Research, Indianapolis, IN 46202 5122, USA
    Biochem Biophys Res Commun 305:826-30. 2003
  10. pmc Relationship between glycogen accumulation and the laforin dual specificity phosphatase
    Wei Wang
    Department of Biochemistry and Molecular Biology, Indiana University School of Medicine, Indianapolis, IN 46202 5122, USA
    Biochem Biophys Res Commun 350:588-92. 2006

Collaborators

Detail Information

Publications11

  1. ncbi request reprint Glycogen synthase sensitivity to insulin and glucose-6-phosphate is mediated by both NH2- and COOH-terminal phosphorylation sites
    A V Skurat
    Department of Biochemistry and Molecular Biology, Indiana University School of Medicine, Indianapolis 46202 USA
    Diabetes 49:1096-100. 2000
    ..In Rat-1 fibroblasts, GSK-3 action is not essential for glycogen synthase activation by insulin, and GSK-3-independent mechanisms also operate...
  2. ncbi request reprint Phosphorylation of Ser640 in muscle glycogen synthase by DYRK family protein kinases
    Alexander V Skurat
    Department of Biochemistry and Molecular Biology, Indiana University School of Medicine, Indianapolis, Indiana 46202, USA
    J Biol Chem 279:2490-8. 2004
    ..The inactivation correlated with phosphorylation of site 3a in glycogen synthase. These results indicate that protein kinase(s) from the DYRK family may be involved in a new mechanism for the regulation of glycogen synthesis...
  3. pmc Interaction between glycogenin and glycogen synthase
    Alexander V Skurat
    Department of Biochemistry and Molecular Biology, Indiana University School of Medicine, Indianapolis, IN 46202 5122, USA
    Arch Biochem Biophys 456:93-7. 2006
    ..We demonstrate that the COOH-terminal fragment of glycogenin can be used as an effective high affinity reagent for the purification of glycogen synthase from skeletal muscle and liver...
  4. pmc Laforin is a glycogen phosphatase, deficiency of which leads to elevated phosphorylation of glycogen in vivo
    Vincent S Tagliabracci
    Department of Biochemistry and Molecular Biology, Indiana University School of Medicine, Indianapolis, IN 46202, USA
    Proc Natl Acad Sci U S A 104:19262-6. 2007
    ..This study provides a molecular link between an observed biochemical property of laforin and the phenotype of a mouse model of Lafora disease. The results also have important implications for glycogen metabolism generally...
  5. ncbi request reprint GNIP, a novel protein that binds and activates glycogenin, the self-glucosylating initiator of glycogen biosynthesis
    Alexander V Skurat
    Department of Biochemistry and Molecular Biology and Center for Diabetes Research, Indiana University School of Medicine, Indianapolis, Indiana 46202, USA
    J Biol Chem 277:19331-8. 2002
    ..GNIPs may represent a novel participant in the initiation of glycogen synthesis...
  6. ncbi request reprint Structure-function analysis of GNIP, the glycogenin-interacting protein
    Lanmin Zhai
    Department of Biochemistry and Molecular Biology, Center for Diabetes Research, Indiana University School of Medicine, 635 Barnhill Drive, Indianapolis, IN 46202 5122, USA
    Arch Biochem Biophys 421:236-42. 2004
    ..Heterologous interactions between GNIP1 and GNIP2 were also detected. Since glycogenin is also a dimer, higher order multimeric complexes between glycogenin and GNIPs would be possible...
  7. pmc Glycogen metabolism in tissues from a mouse model of Lafora disease
    Wei Wang
    Department of Biochemistry and Molecular Biology, Indiana University School of Medicine, Indianapolis, IN 46202 5122, USA
    Arch Biochem Biophys 457:264-9. 2007
    ....
  8. pmc Starch binding domain-containing protein 1/genethonin 1 is a novel participant in glycogen metabolism
    Sixin Jiang
    Department of Biochemistry and Molecular Biology, Indiana University School of Medicine, Indianapolis, Indiana 46202, USA
    J Biol Chem 285:34960-71. 2010
    ..We conclude that Stbd1 is involved in glycogen metabolism by binding to glycogen and anchoring it to membranes, thereby affecting its cellular localization and its intracellular trafficking to lysosomes...
  9. ncbi request reprint Overexpression of glycogen synthase in mouse muscle results in less branched glycogen
    Bartholomew A Pederson
    Department of Biochemistry and Molecular Biology, Indiana University School of Medicine, and Indiana University Center for Diabetes Research, Indianapolis, IN 46202 5122, USA
    Biochem Biophys Res Commun 305:826-30. 2003
    ..However, this compared with an increase in glycogen synthase of some 50-fold, so that the increase in branching enzyme in response to overexpression of glycogen synthase was insufficient to synthesize normally branched glycogen...
  10. pmc Relationship between glycogen accumulation and the laforin dual specificity phosphatase
    Wei Wang
    Department of Biochemistry and Molecular Biology, Indiana University School of Medicine, Indianapolis, IN 46202 5122, USA
    Biochem Biophys Res Commun 350:588-92. 2006
    ..We propose, therefore, that laforin senses cytosolic glycogen accumulation which in turn determines the level of laforin protein...
  11. pmc Control of mammalian glycogen synthase by PAS kinase
    Wayne A Wilson
    Department of Biochemistry, University of Utah School of Medicine, Salt Lake City, UT 84132, USA
    Proc Natl Acad Sci U S A 102:16596-601. 2005
    ..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...