title: Characterization of the binding and phosphorylation of cardiac calsequestrin by epsilon protein kinase C.
abstract: In this study, we report the cloning of the rat cardiac isoform of calsequestrin on the basis of its interaction with an epsilonprotein kinase C-unique sequence (epsilonV1) derived form the epsilonprotein kinase C regulatory domain. Calsequestrin binds activated epsilonprotein kinase C holoenzyme better than the inactive enzyme and nearly three times better than other protein kinase C isozymes. The interaction between epsilonprotein kinase C and calsequestrin is mediated by sequences in both the regulatory and kinase domains of the epsilonprotein kinase C. Finally, we show that calsequestrin is an epsilonprotein kinase C substrate in vitro and protein kinase C phosphorylation of calsequestrin leads to a decreased binding of epsilonprotein kinase C to calsequestrin.
authors.affiliation: Department of Molecular Pharmacology, Stanford University School of Medicine, CA 94305-5332, USA.
authors.forename: M M
authors.initials: MM
authors.lastname: Rodriguez
authors.forename: C H
authors.initials: CH
authors.lastname: Chen
authors.forename: B L
authors.initials: BL
authors.lastname: Smith
authors.forename: D
authors.initials: D
authors.lastname: Mochly-Rosen
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002155:Calsequestrin / Q000235:genetics* / Q000378:metabolism*; D003001:Cloning, Molecular; D007527:Isoenzymes / Q000378:metabolism*; D008969:Molecular Sequence Data; D009206:Myocardium / Q000378:metabolism*; D010766:Phosphorylation; D020033:Protein Isoforms / Q000235:genetics / Q000378:metabolism; D011493:Protein Kinase C / Q000378:metabolism*; D051744:Protein Kinase C-epsilon; D051381:Rats; D017207:Rats, Sprague-Dawley; D016415:Sequence Alignment; D013379:Substrate Specificity
chemical_list: D002155:Calsequestrin; D007527:Isoenzymes; D020033:Protein Isoforms; C497257:Prkce protein, rat; D011493:Protein Kinase C; D051744:Protein Kinase C-epsilon