Interaction between glycogenin and glycogen synthase

Research output: Contribution to journalArticle

20 Scopus citations

Abstract

Glycogen synthase plays a key role in regulating glycogen metabolism. In a search for regulators of glycogen synthase, a yeast two-hybrid study was performed. Two glycogen synthase-interacting proteins were identified in human skeletal muscle, glycogenin-1, and nebulin. The interaction with glycogenin was found to be mediated by the region of glycogenin which contains the 33 COOH-terminal amino acid residues. The regions in glycogen synthase containing both NH2- and COOH-terminal phosphorylation sites are not involved in the interaction. The core segment of glycogen synthase from Glu21 to Gly503 does not bind COOH-terminal fragment of glycogenin. However, this region of glycogen synthase binds full-length glycogenin indicating that glycogenin contains at least one additional interacting site for glycogen synthase besides the COOH-terminus. 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.

Original languageEnglish (US)
Pages (from-to)93-97
Number of pages5
JournalArchives of Biochemistry and Biophysics
Volume456
Issue number1
DOIs
StatePublished - Dec 1 2006

Keywords

  • Glycogen
  • Glycogen synthase
  • Glycogenin
  • Nebulin

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

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