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Decoding of short-lived Ca2+ influx signals into long term substrate phosphorylation through activation of two distinct classes of protein kinase C

Mogami, Hideo, Zhang, Hui, Suzuki, Yoko, Urano, Tetsumei, Saito, Naoaki, Kojima, Itaru and Petersen, Ole Holger ORCID: https://orcid.org/0000-0002-6998-0380 2003. Decoding of short-lived Ca2+ influx signals into long term substrate phosphorylation through activation of two distinct classes of protein kinase C. Journal of Biological Chemistry 278 (11) , pp. 9896-9904. 10.1074/jbc.M210653200

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Abstract

In electrically excitable cells, membrane depolarization opens voltage-dependent Ca2+ channels eliciting Ca2+influx, which plays an important role for the activation of protein kinase C (PKC). However, we do not know whether Ca2+ influx alone can activate PKC. The present study was conducted to investigate the Ca2+ influx-induced activation mechanisms for two classes of PKC, conventional PKC (cPKC; PKCα) and novel PKC (nPKC; PKCθ), in insulin-secreting cells. We have demonstrated simultaneous translocation of both DsRed-tagged PKCα to the plasma membrane and green fluorescent protein (GFP)-tagged myristoylated alanine-rich C kinase substrate to the cytosol as a dual marker of PKC activity in response to depolarization-evoked Ca2+ influx in the DsRed-tagged PKCα and GFP-tagged myristoylated alanine-rich C kinase substrate co-expressing cells. The result indicates that Ca2+ influx can generate diacylglycerol (DAG), because cPKC is activated by Ca2+ and DAG. We showed this in three different ways by demonstrating: 1) Ca2+ influx-induced translocation of GFP-tagged C1 domain of PKCγ, 2) Ca2+influx-induced translocation of GFP-tagged pleckstrin homology domain, and 3) Ca2+ influx-induced translocation of GFP-tagged PKCθ, as a marker of DAG production and/or nPKC activity. Thus, Ca2+ influx alone via voltage-dependent Ca2+ channels can generate DAG, thereby activating cPKC and nPKC, whose activation is structurally independent of Ca2+.

Item Type: Article
Date Type: Publication
Status: Published
Schools: Biosciences
Systems Immunity Research Institute (SIURI)
Publisher: American Society for Biochemistry and Molecular Biology
ISSN: 0021-9258
Last Modified: 27 Oct 2022 08:42
URI: https://orca.cardiff.ac.uk/id/eprint/63145

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