Source:http://linkedlifedata.com/resource/pubmed/id/10473617
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
37
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| pubmed:dateCreated |
1999-10-7
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| pubmed:abstractText |
Activation of the serine kinase protein kinase D (PKD)/PKCmicro is controlled by the phosphorylation of two serine residues within its activation loop via a PKC-dependent signaling cascade. In this study we have identified the C-terminal serine 916 residue as an in vivo phosphorylation site within active PKD/PKCmu. An antibody that recognized PKD/PKCmu proteins specifically phosphorylated on the serine 916 residue was generated and used to show that phosphorylation of Ser-916 is induced by phorbol ester treatment of cells. Thus, the pS916 antibody is a useful tool to study the regulation of PKD/PKCmu activity in vivo. Antigen receptor ligation of T and B lymphocytes also induced phosphorylation of the serine 916 residue of PKD/PKCmu. Furthermore the regulatory FcgammaRIIB receptor, which mediates vital negative feedback signals to the B cell antigen receptor complex, inhibited the antigen receptor-induced activation and serine 916 phosphorylation of PKD/PKCmu. The degree of serine 916 phosphorylation during lymphocyte activation and inhibition exactly correlated with the activation status of PKD/PKCmu. Moreover, using different mutants of PKD/PKCmu, we show that serine 916 is not trans-phosphorylated by an upstream kinase but is rather an autophosphorylation event that occurs following activation of PKD/PKCmu.
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| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/DNA Primers,
http://linkedlifedata.com/resource/pubmed/chemical/Phorbol 12,13-Dibutyrate,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphopeptides,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinase C,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Serine,
http://linkedlifedata.com/resource/pubmed/chemical/protein kinase D
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| pubmed:status |
MEDLINE
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| pubmed:month |
Sep
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| pubmed:issn |
0021-9258
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:day |
10
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| pubmed:volume |
274
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
26543-9
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| pubmed:dateRevised |
2007-11-15
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| pubmed:meshHeading |
pubmed-meshheading:10473617-Amino Acid Sequence,
pubmed-meshheading:10473617-Animals,
pubmed-meshheading:10473617-B-Lymphocytes,
pubmed-meshheading:10473617-Base Sequence,
pubmed-meshheading:10473617-COS Cells,
pubmed-meshheading:10473617-DNA Primers,
pubmed-meshheading:10473617-Mice,
pubmed-meshheading:10473617-Mice, Inbred BALB C,
pubmed-meshheading:10473617-Mutagenesis, Site-Directed,
pubmed-meshheading:10473617-Peptide Mapping,
pubmed-meshheading:10473617-Phorbol 12,13-Dibutyrate,
pubmed-meshheading:10473617-Phosphopeptides,
pubmed-meshheading:10473617-Phosphorylation,
pubmed-meshheading:10473617-Protein Kinase C,
pubmed-meshheading:10473617-Recombinant Proteins,
pubmed-meshheading:10473617-Serine,
pubmed-meshheading:10473617-Substrate Specificity,
pubmed-meshheading:10473617-Tumor Cells, Cultured
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| pubmed:year |
1999
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| pubmed:articleTitle |
Characterization of serine 916 as an in vivo autophosphorylation site for protein kinase D/Protein kinase Cmu.
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| pubmed:affiliation |
Lymphocyte Activation Laboratory, Imperial Cancer Research Fund, Lincoln's Inn Fields, London WC2A 3PX, United Kingdom.
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| pubmed:publicationType |
Journal Article
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