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Abstract
RBCK1, a Protein Kinase CβI (PKCβI)-interacting Protein, Regulates PKCβ-dependent Function
Highlights
1650 JOURNAL OF BIOLOGICAL CHEMISTRY tion depends on phosphatidylserine and diacylglycerol and to different extents on calcium and other lipid second messengers
The interaction between RBCK1 and protein kinase CI (PKCI) was assessed by immunoprecipitating endogenous protein kinase C (PKC)I using an anti-PKCI antibody followed by Western blot analysis of the immunoprecipitates with an anti-green fluorescent protein (GFP) antibody
Similar amounts of endogenous PKCI were immunoprecipitated (Fig. 1A), the amounts of RBCK1-GFP co-immunoprecipitated with PKCI increased after a 1-min treatment with 5 M phenylephrine followed by a decline 3 min after stimulation (Fig. 1, A and B)
Summary
1650 JOURNAL OF BIOLOGICAL CHEMISTRY tion depends on phosphatidylserine and diacylglycerol and to different extents on calcium and other lipid second messengers. We first set out to determine whether RBCK1 binds PKCI in neonatal cardiac myocytes and whether PKC activation with phenylephrine regulates their interaction. Increased Interaction between PKCI and RBCK1 after Prolonged Phenylephrine Treatment—Prolonged treatment of cardiac myocytes with phorbol 12-myristate 13-acetate or phenylephrine causes increased cell size, which was shown to be dependent on PKC activation [15].
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