| pubmed-article:17724026 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:17724026 | lifeskim:mentions | umls-concept:C0018787 | lld:lifeskim |
| pubmed-article:17724026 | lifeskim:mentions | umls-concept:C0031715 | lld:lifeskim |
| pubmed-article:17724026 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:17724026 | lifeskim:mentions | umls-concept:C0256813 | lld:lifeskim |
| pubmed-article:17724026 | lifeskim:mentions | umls-concept:C1704735 | lld:lifeskim |
| pubmed-article:17724026 | lifeskim:mentions | umls-concept:C0679622 | lld:lifeskim |
| pubmed-article:17724026 | lifeskim:mentions | umls-concept:C0205314 | lld:lifeskim |
| pubmed-article:17724026 | pubmed:issue | 42 | lld:pubmed |
| pubmed-article:17724026 | pubmed:dateCreated | 2007-10-15 | lld:pubmed |
| pubmed-article:17724026 | pubmed:abstractText | 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 PKCepsilon and zeta and troponin T (cTnT) associated with PKC alpha, delta, and epsilon. Based on its association with cTnI, we hypothesized that PKCzeta 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 PKCzeta: 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 PKCzeta using PKC phospho-motif antibodies to determine the phosphorylation 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 PKCzeta T560E. Ser phosphorylation of tropomyosin was increased by all three active mutants of PKCzeta. Ser/Thr phosphorylation of myosin-binding protein C increased primarily by PKCzeta A119E. Both PKCzeta A119E and T410E mutants increased desmin Ser/Thr phosphorylation. To explain the apparent Thr dephosphorylation of cTnI and cTnT, we hypothesized that PKCzeta 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 PKCzeta is a novel regulator of myofilament protein phosphorylation. | lld:pubmed |
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| pubmed-article:17724026 | pubmed:language | eng | lld:pubmed |
| pubmed-article:17724026 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17724026 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:17724026 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:17724026 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:17724026 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:17724026 | pubmed:author | pubmed-author:SolaroR... | lld:pubmed |
| pubmed-article:17724026 | pubmed:author | pubmed-author:WuSteven CSC | lld:pubmed |
| pubmed-article:17724026 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:17724026 | pubmed:day | 19 | lld:pubmed |
| pubmed-article:17724026 | pubmed:volume | 282 | lld:pubmed |
| pubmed-article:17724026 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:17724026 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:17724026 | pubmed:pagination | 30691-8 | lld:pubmed |
| pubmed-article:17724026 | pubmed:dateRevised | 2010-12-3 | lld:pubmed |
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| pubmed-article:17724026 | pubmed:year | 2007 | lld:pubmed |
| pubmed-article:17724026 | pubmed:articleTitle | Protein kinase C zeta. A novel regulator of both phosphorylation and de-phosphorylation of cardiac sarcomeric proteins. | lld:pubmed |
| pubmed-article:17724026 | pubmed:affiliation | Center for Cardiovascular Research, Department of Physiology and Biophysics, University of Illinois at Chicago College of Medicine, Chicago, Illinois 60612, USA. | lld:pubmed |
| pubmed-article:17724026 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:17724026 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:17724026 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| pubmed-article:17724026 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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