Phosphorylation of histones and non-histone nuclear proteins in liver cells stimulated by glucagon and cyclic AMP.
Phosphorylation of a characteristic subset of nuclear proteins is increased in rat liver cells stimulated with glucagon. Regulated proteins include histones H1 and H3, an HMG 14-like protein and a previously unidentified 23-kDa basic protein. The effect of glucagon is mimicked by forskolin and exogenous cAMP. Insulin and dexamethasone have no effect. In a cell-free system containing purified hepatocyte nuclei, addition of cAMP-dependent protein kinase results in phosphorylation of histone H3, an HMG 14-like protein and a 23-kDa basic protein similar or identical to the protein phosphorylated in vivo.
D000818:Animals; D002474:Cell-Free System; D002868:Chromosomal Proteins, Non-Histone / Q000378:metabolism*; D005576:Colforsin; D000242:Cyclic AMP / Q000494:pharmacology*; D004224:Diterpenes / Q000494:pharmacology; D004591:Electrophoresis, Polyacrylamide Gel; D005934:Glucagon / Q000494:pharmacology*; D006657:Histones / Q000378:metabolism*; D008099:Liver / Q000187:drug effects / Q000378:metabolism*; D008970:Molecular Weight; D010766:Phosphorylation; D051381:Rats
D002868:Chromosomal Proteins, Non-Histone; D004224:Diterpenes; D006657:Histones; D005576:Colforsin; D005934:Glucagon; D000242:Cyclic AMP