Subtype-Specific Translocation of the δ Subtype of Protein Kinase C and Its Activation by Tyrosine Phosphorylation Induced by Ceramide in HeLa Cells

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Published inMolecular and Cellular Biology Vol. 21; no. 5; pp. 1769 - 1783
Main Authors Kajimoto, Taketoshi, Ohmori, Shiho, Shirai, Yasuhito, Sakai, Norio, Saito, Naoaki
Format Journal Article
LanguageEnglish
Published United States American Society for Microbiology 01.03.2001
Taylor & Francis
Subjects
Adenoviridae - genetics
Animals
Antineoplastic Agents - pharmacology
Cell Fractionation
Cell Growth and Development
Cell Line
Cell Membrane - metabolism
Ceramides - metabolism
Ceramides - pharmacology
CHO Cells
Cricetinae
Diglycerides - metabolism
Enzyme Activation
Enzyme Inhibitors - pharmacology
Golgi Apparatus - metabolism
Green Fluorescent Proteins
HeLa Cells
Humans
Immunoblotting
Interferon-gamma - metabolism
Isoenzymes - metabolism
Luminescent Proteins - metabolism
Magnesium - metabolism
Phorbol Esters - pharmacology
Phosphatidylserines - metabolism
Phosphorylation
Precipitin Tests
Protein Kinase C - metabolism
Protein Kinase C-alpha
Protein Kinase C-delta
protein translocation
Protein Transport
Recombinant Fusion Proteins - metabolism
Signal Transduction
Sphingomyelin Phosphodiesterase - metabolism
Sphingosine - analogs & derivatives
Sphingosine - pharmacology
Time Factors
Tyrosine - metabolism
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Abstract Article Usage Stats Services MCB Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon Twitter current issue Spotlights in the Current Issue MCB About MCB Subscribers Authors Reviewers Advertisers Inquiries from the Press Permissions & Commercial Reprints ASM Journals Public Access Policy MCB RSS Feeds 1752 N Street N.W. • Washington DC 20036 202.737.3600 • 202.942.9355 fax • journals@asmusa.org Print ISSN: 0270-7306 Online ISSN: 1098-5549 Copyright © 2014 by the American Society for Microbiology.   For an alternate route to MCB .asm.org, visit: MCB       
AbstractList 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 δPKC-GFP to the Golgi complex, while αPKC- and ζPKC-GFP did not respond to ceramide. The Golgi-associated δPKC-GFP induced by ceramide was further translocated to the plasma membrane by phorbol ester treatment. Ceramide itself accumulated to the Golgi complex where δPKC was translocated by ceramide. Gamma interferon also induced the δPKC-specific translocation from the cytoplasm to the Golgi complex via the activation of Janus kinase and Mg 2+ -dependent neutral sphingomyelinase. Photobleaching studies showed that ceramide does not evoke tight binding of δPKC-GFP to the Golgi complex but induces the continuous association and dissociation of δPKC with the Golgi complex. Ceramide inhibited the kinase activity of δPKC-GFP in the presence of phosphatidylserine and diolein in vitro, while the kinase activity of δPKC-GFP immunoprecipitated from ceramide-treated cells was increased. The immunoprecipitated δPKC-GFP was tyrosine phosphorylated after ceramide treatment. Tyrosine kinase inhibitor abolished the ceramide-induced activation and tyrosine phosphorylation of δPKC-GFP. These results suggested that gamma interferon stimulation followed by ceramide generation through Mg 2+ -dependent sphingomyelinase induced δPKC-specific translocation to the Golgi complex and that translocation results in δPKC activation through tyrosine phosphorylation of the enzyme.
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 where delta 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 Mg(2+)-dependent neutral sphingomyelinase. Photobleaching studies showed that ceramide does not evoke tight binding of delta PKC-GFP to the Golgi complex but induces the continuous association and dissociation of delta PKC with the Golgi complex. Ceramide inhibited the kinase activity of delta PKC-GFP in the presence of phosphatidylserine and diolein in vitro, while the kinase activity of delta PKC-GFP immunoprecipitated from ceramide-treated cells was increased. The immunoprecipitated delta 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 Mg(2+)-dependent sphingomyelinase induced delta PKC-specific translocation to the Golgi complex and that translocation results in delta PKC activation through tyrosine phosphorylation of the enzyme.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 where delta 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 Mg(2+)-dependent neutral sphingomyelinase. Photobleaching studies showed that ceramide does not evoke tight binding of delta PKC-GFP to the Golgi complex but induces the continuous association and dissociation of delta PKC with the Golgi complex. Ceramide inhibited the kinase activity of delta PKC-GFP in the presence of phosphatidylserine and diolein in vitro, while the kinase activity of delta PKC-GFP immunoprecipitated from ceramide-treated cells was increased. The immunoprecipitated delta 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 Mg(2+)-dependent sphingomyelinase induced delta PKC-specific translocation to the Golgi complex and that translocation results in delta PKC activation through tyrosine phosphorylation of the enzyme.
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 sub(2)-ceramide but not C sub(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 where delta 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 Mg super(2+)-dependent neutral sphingomyelinase. Photobleaching studies showed that ceramide does not evoke tight binding of delta PKC-GFP to the Golgi complex but induces the continuous association and dissociation of delta PKC with the Golgi complex. Ceramide inhibited the kinase activity of delta PKC-GFP in the presence of phosphatidylserine and diolein in vitro, while the kinase activity of delta PKC-GFP immunoprecipitated from ceramide-treated cells was increased. The immunoprecipitated delta 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 Mg super(2+)-dependent sphingomyelinase induced delta PKC-specific translocation to the Golgi complex and that translocation results in delta PKC activation through tyrosine phosphorylation of the enzyme.
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 where delta 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 Mg(2+)-dependent neutral sphingomyelinase. Photobleaching studies showed that ceramide does not evoke tight binding of delta PKC-GFP to the Golgi complex but induces the continuous association and dissociation of delta PKC with the Golgi complex. Ceramide inhibited the kinase activity of delta PKC-GFP in the presence of phosphatidylserine and diolein in vitro, while the kinase activity of delta PKC-GFP immunoprecipitated from ceramide-treated cells was increased. The immunoprecipitated delta 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 Mg(2+)-dependent sphingomyelinase induced delta PKC-specific translocation to the Golgi complex and that translocation results in delta PKC activation through tyrosine phosphorylation of the enzyme.
Article Usage Stats Services MCB Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon Twitter current issue Spotlights in the Current Issue MCB About MCB Subscribers Authors Reviewers Advertisers Inquiries from the Press Permissions & Commercial Reprints ASM Journals Public Access Policy MCB RSS Feeds 1752 N Street N.W. • Washington DC 20036 202.737.3600 • 202.942.9355 fax • journals@asmusa.org Print ISSN: 0270-7306 Online ISSN: 1098-5549 Copyright © 2014 by the American Society for Microbiology.   For an alternate route to MCB .asm.org, visit: MCB       
Author Shiho Ohmori
Naoaki Saito
Norio Sakai
Taketoshi Kajimoto
Yasuhito Shirai
AuthorAffiliation Laboratory of Molecular Pharmacology, Biosignal Research Center, Kobe University, Nada-ku, Kobe 657-8501, Japan
AuthorAffiliation_xml – name: Laboratory of Molecular Pharmacology, Biosignal Research Center, Kobe University, Nada-ku, Kobe 657-8501, Japan
Author_xml – sequence: 1
  givenname: Taketoshi
  surname: Kajimoto
  fullname: Kajimoto, Taketoshi
  organization: Laboratory of Molecular Pharmacology, Biosignal Research Center, Kobe University
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  givenname: Shiho
  surname: Ohmori
  fullname: Ohmori, Shiho
  organization: Laboratory of Molecular Pharmacology, Biosignal Research Center, Kobe University
– sequence: 3
  givenname: Yasuhito
  surname: Shirai
  fullname: Shirai, Yasuhito
  organization: Laboratory of Molecular Pharmacology, Biosignal Research Center, Kobe University
– sequence: 4
  givenname: Norio
  surname: Sakai
  fullname: Sakai, Norio
  organization: Laboratory of Molecular Pharmacology, Biosignal Research Center, Kobe University
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  givenname: Naoaki
  surname: Saito
  fullname: Saito, Naoaki
  email: naosaito@kobe-u.ac.jp
  organization: Laboratory of Molecular Pharmacology, Biosignal Research Center, Kobe University
BackLink https://www.ncbi.nlm.nih.gov/pubmed/11238914$$D View this record in MEDLINE/PubMed
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Corresponding author. Mailing address: Laboratory of Molecular Pharmacology, Biosignal Research Center, Kobe University, 1-1 Rokkodai-cho, Nada-ku, Kobe 657-8501, Japan. Phone: 81-78-803-5961. Fax: 81-78-803-5971. E-mail: naosaito@kobe-u.ac.jp.
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We investigated the functional roles of ceramide, an intracellular lipid mediator, in cell signaling pathways by monitoring the intracellular movement of...
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SubjectTerms Adenoviridae - genetics
Animals
Antineoplastic Agents - pharmacology
Cell Fractionation
Cell Growth and Development
Cell Line
Cell Membrane - metabolism
Ceramides - metabolism
Ceramides - pharmacology
CHO Cells
Cricetinae
Diglycerides - metabolism
Enzyme Activation
Enzyme Inhibitors - pharmacology
Golgi Apparatus - metabolism
Green Fluorescent Proteins
HeLa Cells
Humans
Immunoblotting
Interferon-gamma - metabolism
Isoenzymes - metabolism
Luminescent Proteins - metabolism
Magnesium - metabolism
Phorbol Esters - pharmacology
Phosphatidylserines - metabolism
Phosphorylation
Precipitin Tests
Protein Kinase C - metabolism
Protein Kinase C-alpha
Protein Kinase C-delta
protein translocation
Protein Transport
Recombinant Fusion Proteins - metabolism
Signal Transduction
Sphingomyelin Phosphodiesterase - metabolism
Sphingosine - analogs & derivatives
Sphingosine - pharmacology
Time Factors
Tyrosine - metabolism
Title Subtype-Specific Translocation of the δ Subtype of Protein Kinase C and Its Activation by Tyrosine Phosphorylation Induced by Ceramide in HeLa Cells
URI http://mcb.asm.org/content/21/5/1769.abstract
https://www.tandfonline.com/doi/abs/10.1128/MCB.21.5.1769-1783.2001
https://www.ncbi.nlm.nih.gov/pubmed/11238914
https://www.proquest.com/docview/17760686
https://www.proquest.com/docview/76953545
https://pubmed.ncbi.nlm.nih.gov/PMC86731
Volume 21
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