Amino acid sequence and expression of the hepatic glycogen-binding (GL-subunit of protein phosphatase-1

Martin J. Doherty; Greg Moorhead; Nick Morrice; Philip Cohen; Patricia T.W. Cohen

doi:10.1016/0014-5793(95)01184-G

Amino acid sequence and expression of the hepatic glycogen-binding (G_L-subunit of protein phosphatase-1

Martin J. Doherty, Greg Moorhead, Nick Morrice, Philip Cohen, Patricia T.W. Cohen

Research output: Contribution to journal › Article › peer-review

141 Citations (Scopus)

Abstract

A full-length cDNA encoding the putative hepatic glycogen-binding (G_L) 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 (G_M) subunit of PP1 from striated muscle. The similarities between G_M and G_L were most striking between residues 63-86, 144-166 and 186-227 of human G_M (∼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 G_L.

Original language	English
Pages (from-to)	294-298
Number of pages	5
Journal	FEBS Letters
Volume	375
Issue number	3
DOIs	https://doi.org/10.1016/0014-5793(95)01184-G
Publication status	Published - 20 Nov 1995

Keywords

Cyclic AMP-dependent protein kinase
Glycogen
Glycogen metabolism
Protein phosphatase
Targetting subunit

ASJC Scopus subject areas

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

Access to Document

10.1016/0014-5793(95)01184-GLicence: No Licence / Unknown

Cite this

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title = "Amino acid sequence and expression of the hepatic glycogen-binding (GL-subunit of protein phosphatase-1",

abstract = "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 (∼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.",

keywords = "Cyclic AMP-dependent protein kinase, Glycogen, Glycogen metabolism, Protein phosphatase, Targetting subunit",

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AU - Doherty, Martin J.

AU - Moorhead, Greg

AU - Morrice, Nick

AU - Cohen, Philip

AU - Cohen, Patricia T.W.

PY - 1995/11/20

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