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Structure and expression of the Caenorhabditis elegans protein kinase C2 gene. Origins and regulated expression of a family of Ca2+-activated protein kinase C isoforms.
Islas-Trejo, A; Land, M; Tcherepanova, I; Freedman, J H; Rubin, C S.
Afiliación
  • Islas-Trejo A; Department of Molecular Pharmacology, Atran Laboratories, Albert Einstein College of Medicine, Bronx, New York 10461, USA.
J Biol Chem ; 272(10): 6629-40, 1997 Mar 07.
Article en En | MEDLINE | ID: mdl-9045693
The molecular and cellular basis for concerted Ca2+/lipid signaling in Caenorhabditis elegans was investigated. A unique gene (pkc-2) and cognate cDNAs that encode six Ca2+/diacylglycerol-stimulated PKC2 isoenzymes were characterized. PKC2 polypeptides (680-717 amino acid residues) share identical catalytic, Ca2+-binding, diacylglycerol-activation and pseudosubstrate domains. However, sequences of the N- and C-terminal regions of the kinases diverge. PKC2 diversity is partly due to differential activation of transcription by distinct promoters. Each promoter precedes an adjacent exon that encodes 5'-untranslated RNA, an initiator AUG codon and a unique open reading frame. PKC2 mRNAs also incorporate one of two 3'-terminal exons via alternative splicing. Cells that are capable of receiving and propagating signals carried by Ca2+/diacylglycerol were identified by assessing activities of pkc-2 gene promoters in transgenic C. elegans and visualizing the distribution of PKC2 polypeptides via immunofluorescence. Highly-selective expression of certain PKC2 isoforms was observed in distinct subsets of neurons, intestinal and muscle cells. A low level of PKC2 isoforms is observed in embryos. When L1 larvae hatch and interact with the external environment PKC2 content increases 10-fold. Although 77- and 78-kDa PKC2 isoforms are evident throughout post-embryonic development, an 81-kDa isoform appears to be adapted for function in L1 and L2 larvae.
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Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Proteína Quinasa C / Genes de Helminto / Caenorhabditis elegans / Proteínas de Caenorhabditis elegans / Isoenzimas Límite: Animals Idioma: En Revista: J Biol Chem Año: 1997 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Estados Unidos
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Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Proteína Quinasa C / Genes de Helminto / Caenorhabditis elegans / Proteínas de Caenorhabditis elegans / Isoenzimas Límite: Animals Idioma: En Revista: J Biol Chem Año: 1997 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Estados Unidos