PMID: 2108025Mar 10, 1990Paper

Localization of phosphoserine residues in the alpha subunit of rabbit skeletal muscle phosphorylase kinase

European Journal of Biochemistry
H E MeyerL M Heilmeyer

Abstract

The alpha subunit of skeletal muscle phosphorylase kinase, as isolated, carries phosphate at the serine residues 1018, 1020 and 1023. Employing the S-ethyl-cysteine method, these residues are found to be phosphorylated partially, i.e. differently phosphorylated species exist in muscle. Serine 1018 is a site which can be phosphorylated by the cyclic-AMP-dependent protein kinase. The serine residues 972, 985 and 1007 are phosphorylated by phosphorylase kinase itself when its activity is stimulated by micromolar concentrations of Ca2+. These phosphorylation sites are not identical to those found to be phosphorylated already in the enzyme as prepared from freshly excised muscle. A 'multiphosphorylation loop' uniquely present in this but not in the homologous beta subunit contains all the phosphoserine residues so far identified in the alpha subunit.

References

Aug 1, 1977·Proceedings of the National Academy of Sciences of the United States of America·T M Lincoln, J D Corbin
Dec 1, 1988·Proceedings of the National Academy of Sciences of the United States of America·M W KilimannL M Heilmeyer
May 1, 1988·Proceedings of the National Academy of Sciences of the United States of America·N F ZanderM W Kilimann
Jul 27, 1984·Journal of Chromatography·J W Crabb, L M Heilmeyer

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Citations

Nov 1, 1993·Molecular and Cellular Biochemistry·L M HeilmeyerH P Jennissen
Mar 15, 1992·Proceedings of the National Academy of Sciences of the United States of America·J J DavidsonM W Kilimann
Aug 11, 2000·Biological Chemistry·A BeyerL M Heilmeyer
Feb 22, 2012·PloS One·Gisela Nogales-GadeaAntoni L Andreu
Apr 17, 1992·Biochimica Et Biophysica Acta·K E JaegerU K Winkler
Sep 13, 1991·Biochimica Et Biophysica Acta·L M Heilmeyer
Aug 15, 1991·Biochemical and Biophysical Research Communications·H DaubeH J Schramm

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