RBCK1, a Protein Kinase CβI (PKCβI)-interacting Protein, Regulates PKCβ-dependent Function

Alice Vallentin,Daria Mochly-Rosen

doi:10.1074/jbc.m601710200

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 C␤I (PKC␤I) was assessed by immunoprecipitating endogenous protein kinase C (PKC)␤I using an anti-PKC␤I antibody followed by Western blot analysis of the immunoprecipitates with an anti-green fluorescent protein (GFP) antibody
Similar amounts of endogenous PKC␤I were immunoprecipitated (Fig. 1A), the amounts of RBCK1-GFP co-immunoprecipitated with PKC␤I increased after a 1-min treatment with 5 ␮M phenylephrine followed by a decline 3 min after stimulation (Fig. 1, A and B)

Summary

Introduction

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 PKC␤I in neonatal cardiac myocytes and whether PKC activation with phenylephrine regulates their interaction. Increased Interaction between PKC␤I 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].

Results

Conclusion