Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
Subtype-specific translocation of the delta subtype of protein kinase C and its activation by tyrosine phosphorylation induced by ceramide in HeLa cells
Autore:
Kajimoto, T; Ohmori, S; Shirai, Y; Sakai, N; Saito, N;
Indirizzi:
Kobe Univ, Biosignal Res Ctr, Mol Pharmacol Lab, Nada Ku, Kobe, Hyogo 6578501, Japan Kobe Univ Kobe Hyogo Japan 6578501 b, Nada Ku, Kobe, Hyogo 6578501, Japan
Titolo Testata:
MOLECULAR AND CELLULAR BIOLOGY
fascicolo: 5, volume: 21, anno: 2001,
pagine: 1769 - 1783
SICI:
0270-7306(200103)21:5<1769:STOTDS>2.0.ZU;2-N
Fonte:
ISI
Lingua:
ENG
Soggetto:
SIGNAL-TRANSDUCTION PATHWAY; GREEN FLUORESCENT PROTEIN; NECROSIS-FACTOR-ALPHA; GAMMA-MUTANT MICE; GROWTH-FACTOR; PROTEOLYTIC ACTIVATION; SPHINGOMYELIN TURNOVER; NEUROTROPHIN RECEPTOR; CELLULAR-RESPONSES; GOLGI-APPARATUS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
66
Recensione:
Indirizzi per estratti:
Indirizzo: Saito, N Kobe Univ, Biosignal Res Ctr, Mol Pharmacol Lab, Nada Ku, 1-1 Rokkodai Cho, Kobe, Hyogo 6578501, Japan Kobe Univ 1-1 Rokkodai Cho Kobe HyogoJapan 6578501 578501, Japan
Citazione:
T. Kajimoto et al., "Subtype-specific translocation of the delta subtype of protein kinase C and its activation by tyrosine phosphorylation induced by ceramide in HeLa cells", MOL CELL B, 21(5), 2001, pp. 1769-1783

Abstract

We investigated the functional roles of ceramide, an intracellular lipid mediator, in cell signaling pathways by monitoring the intracellular movement of protein kinase C (PKC) subtypes fused to green fluorescent protein (GFP) in HeLa living cells. C-2-ceramide but not C-2-dihydroceramide induced translocation of delta PKC-GFP to the Golgi complex, while alpha PKC- and zeta PKC-GFP did not respond to ceramide. The Golgi-associated delta PKC-GFP induced by ceramide was further translocated to the plasma membrane by phorbol ester treatment. Ceramide itself accumulated to the Golgi complex wheredelta PKC was translocated by ceramide. Gamma interferon also induced the delta PKC-specific translocation from the cytoplasm to the Golgi complex via the activation of Janus kinase and Mg2+-dependent neutral sphingomyelinase. Photobleaching studies showed that ceramide does not evoke tight bindingof delta PKC-GFP to the Golgi complex but induces the continuous association and dissociation of delta PKC with the Golgi complex. Ceramide inhibitedthe kinase activity of delta PKC-GFP in the presence of phosphatidylserineand diolein in vitro, while the kinase activity of delta PKC-GFP immunoprecipitated from ceramide-treated cells was increased. The immunoprecipitateddelta PKC-GFP was tyrosine phosphorylated after ceramide treatment. Tyrosine kinase inhibitor abolished the ceramide-induced activation and tyrosine phosphorylation of delta PKC-GFP. These results suggested that gamma interferon stimulation followed by ceramide generation through Mg2+-dependent sphingomyelinase induced delta PKC-specific translocation to the Golgi complexand that translocation results in delta PKC activation through tyrosine phosphorylation of the enzyme.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 03/07/20 alle ore 16:43:57