NDLI: Protein Kinase C ζ: A NOVEL REGULATOR OF BOTH PHOSPHORYLATION AND DE-PHOSPHORYLATION OF CARDIAC SARCOMERIC PROTEINS* S

Content Provider	PubMed Central
Author	Wu, Steven C. Solaro, R. John
Abstract	Our experiments investigated associations of specific isoforms of protein kinase C (PKC) with individual proteins in the cardiac troponin complex. Troponin I (cTnI) associated with PKC ε and ζ and troponin T (cTnT) associated with PKC α, δ, and ε. Based on its association with cTnI, we hypothesized that PKCζ is a major regulator of myofilament protein phosphorylation. To test this, we infected adult cardiac myocytes with adenoviral constructs containing DsRed monomer-tagged wild type (WT) and the following constitutively active forms of PKCζ: the pseudo-substrate region (A119E), 3′-phospho-inositide-dependent kinase-1 (T410E), and auto-phosphorylation (T560E). The A119E and T410E mutants displayed increased localization to the Z-discs compared with WT and T560E. Immunoprecipitations were performed in myocytes expressing PKCζ using PKC phospho-motif antibodies to determine the phosphophorylation of cTnI, cTnT, tropomyosin, myosin-binding protein C, and desmin. We did not find serine (Ser) phosphorylation of cTnI or cTnT. However, we observed a significant decrease in threonine (Thr) phosphorylation of cTnI and cTnT notably by PKCζ T560E. Ser phosphorylation of tropomyosin was increased by all three active mutants of PKCζ. Ser/Thr phosphorylation of myosin-binding protein C increased primarily by PKCζ A119E. Both PKCζ A119E and T410E mutants increased desmin Ser/Thr phosphorylation. To explain the apparent Thr dephosphorylation of cTnI and cTnT, we hypothesized that PKCζ exists as a complex with p21-activated kinase-1 (Pak1) and protein phosphatase 2A (PP2A), and this was confirmed by immunoprecipitation Western blot. Our data demonstrate that PKCζ is a novel regulator of myofilament protein phosphorylation.
Related Links	http://dx.doi.org/10.1074/jbc.m703670200
Ending Page	30698
Page Count	8
Starting Page	30691
File Format	PDF
ISSN	00219258
e-ISSN	1083351X
Journal	The Journal of biological chemistry
Issue Number	42
Volume Number	282
Language	English
Publisher Date	2007-08-01
Access Restriction	Open
Subject Keyword	Cell Biology Biochemistry Molecular Biology Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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