Journal article
Insulin Activates a p21-activated Kinase in Muscle Cells via Phosphatidylinositol 3-Kinase*
Abstract
Insulin activates rapidly a complex cascade of lipid and protein kinases leading to stimulation of mitogenic and metabolic events. Here we describe a renaturable kinase of 65 kDa (PK65) that becomes rapidly activated by insulin in differentiated L6 muscle cells (myotubes) and can phosphorylate histones immobilized in polyacrylamide gels. Insulin activation of PK65 was abolished by the tyrosine kinase inhibitor erbstatin and by the …
Authors
Tsakiridis T; Taha C; Grinstein S; Klip A
Journal
Journal of Biological Chemistry, Vol. 271, No. 33, pp. 19664–19667
Publisher
Elsevier
Publication Date
August 1996
DOI
10.1074/jbc.271.33.19664
ISSN
0021-9258
Fields of Research (FoR)
Medical Subject Headings (MeSH)
AnimalsCalcium-Calmodulin-Dependent Protein KinasesCell LineCells, CulturedEnzyme ActivationEnzyme InhibitorsHydroquinonesImmunologic TechniquesInsulinMolecular WeightMuscle, SkeletalPhosphatidylinositol 3-KinasesPhosphotransferases (Alcohol Group Acceptor)PhosphotyrosineProtamine KinaseProtein Serine-Threonine KinasesProto-Oncogene Proteins p21(ras)RatsReceptor, InsulinRibosomal Protein S6 KinasesSignal Transduction