| First Author | Skurat AV | Year | 2006 |
| Journal | Arch Biochem Biophys | Volume | 456 |
| Issue | 1 | Pages | 93-7 |
| PubMed ID | 17055998 | Mgi Jnum | J:116253 |
| Mgi Id | MGI:3693392 | Doi | 10.1016/j.abb.2006.09.024 |
| Citation | Skurat AV, et al. (2006) Interaction between glycogenin and glycogen synthase. Arch Biochem Biophys 456(1):93-7 |
| abstractText | 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 NH(2)- and COOH-terminal phosphorylation sites are not involved in the interaction. The core segment of glycogen synthase from Glu(21) to Gly(503) 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. |
