First Author | Doherty MJ | Year | 1995 |
Journal | FEBS Lett | Volume | 375 |
Issue | 3 | Pages | 294-8 |
PubMed ID | 7498521 | Mgi Jnum | J:45630 |
Mgi Id | MGI:1195785 | Doi | 10.1016/0014-5793(95)01184-g |
Citation | Doherty MJ, et al. (1995) Amino acid sequence and expression of the hepatic glycogen-binding (GL)-subunit of protein phosphatase-1. FEBS Lett 375(3):294-8 |
abstractText | A full-length cDNA encoding the putative hepatic glycogen-binding (GL) subunit of protein phosphatase-1 (PP1) was isolated from a rat liver library. The deduced amino acid sequence (284 residues, 32.6 kDa) was 23% identical (39% similar) to the N-terminal region of the glycogen-binding (GM) subunit of PP1 from striated muscle. The similarities between GM and GL were most striking between residues 63-86, 144-166 and 186-227 of human GM (approximately 40% identity), nearly all the identities with the putative yeast homologue GAC1 being located between 144-166 and 186-227. The cDNA was expressed in E. coli, and the expressed protein transformed the properties of PP1 to those characteristic of the hepatic glycogen-associated enzyme. These experiments establish that the cloned protein is GL. |