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• W2076296913 endingPage "2151" @default.
• W2076296913 startingPage "2140" @default.
• W2076296913 abstract "Protein kinase C-epsilon (PKC-epsilon) plays a central role in cardiac cell signaling, but mechanisms of translocation and anchoring upon activation are poorly understood. Conventional PKC isoforms rely on a rapid Ca2+-mediated recruitment to cell membranes, but this mechanism cannot be employed by PKC-epsilon or other PKC isoforms lacking a Ca2+-binding domain. In this study, we used recombinant green fluorescent protein (GFP) fusion constructs and confocal microscopy to examine the localization, kinetics, and reversibility of PKC-epsilon anchoring in permeabilized rat cardiac myocytes. PKC-epsilon-GFP bound with a striated pattern that co-localized with alpha-actinin, a marker of the Z-line of the sarcomere. Binding required activation of PKC and occurred slowly but reversibly with apparent rate constants of k(on) = 4.6 +/- 1.2 x 10(3) M(-1) x s(-1) and k(off) = 1.4 +/- 0.5 x 10(-3) s(-1) (t1/2 = 8 min) as determined by fluorescence recovery after photobleaching and by perfusion experiments. A truncated construct composed of the N-terminal 144-amino-acid variable region of PKC-epsilon (epsilonV1-GFP), but not an analogous N-terminal domain of PKC-delta, mimicked the Z-line decoration and slow binding rate of the full-length enzyme. These findings suggest that the epsilonV1 domain is important in determining PKC-epsilon localization and translocation kinetics in cardiac muscle. Moreover, PKC-epsilon translocation is not a diffusion-controlled binding process but instead may be limited by intramolecular conformational changes within the V1 domain. The k(off) for epsilonV1-GFP was two- to threefold faster than for full-length enzyme, indicating that other domains in PKC-epsilon contribute to anchoring by prolonging the bound state." @default.
• W2076296913 created "2016-06-24" @default.
• W2076296913 creator A5007872868 @default.
• W2076296913 creator A5057316967 @default.
• W2076296913 creator A5068004698 @default.
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• W2076296913 date "2001-05-01" @default.
• W2076296913 modified "2023-10-16" @default.
• W2076296913 title "Localization and Kinetics of Protein Kinase C-Epsilon Anchoring in Cardiac Myocytes" @default.
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• W2076296913 doi "https://doi.org/10.1016/s0006-3495(01)76187-5" @default.
• W2076296913 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/1301406" @default.
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