ArticleProceedings of the National Academy of Sciences of the United States of America1995
Tyrosine phosphorylation of protein kinase C-delta in response to the activation of the high-affinity receptor for immunoglobulin E modifies its substrate recognition.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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10 citing papers in PubMed, 73 citations in OpenAlex.
- Environmental neurotoxic pesticide dieldrin activates a non receptor tyrosine kinase to promote PKCδ-mediated dopaminergic apoptosis in a dopaminergic neuronal cell model.Neurotoxicology · 2011Article
- Phosphorylation of protein kinase Cdelta on distinct tyrosine residues induces sustained activation of Erk1/2 via down-regulation of MKP-1: role in the apoptotic effect of etoposide.The Journal of biological chemistry · 2008Article
- Tyrosine phosphorylation of protein kinase Cdelta is essential for its apoptotic effect in response to etoposide.Molecular and cellular biology · 2002Article
- Structure-function analysis of Lyn kinase association with lipid rafts and initiation of early signaling events after Fcepsilon receptor I aggregation.Molecular and cellular biology · 2001Article
- Nerve growth factor stimulates multisite tyrosine phosphorylation and activation of the atypical protein kinase C's via a src kinase pathway.Molecular and cellular biology · 2001Article
- Phosphorylation sites of protein kinase C delta in H2O2-treated cells and its activation by tyrosine kinase in vitro.Proceedings of the National Academy of Sciences of the United States of America · 2001Article
- Protein kinase Cdelta targets mitochondria, alters mitochondrial membrane potential, and induces apoptosis in normal and neoplastic keratinocytes when overexpressed by an adenoviral vector.Molecular and cellular biology · 1999Article
- Protein kinase C-delta is an important signaling molecule in insulin-like growth factor I receptor-mediated cell transformation.Molecular and cellular biology · 1998Article
- Activation of protein kinase C by tyrosine phosphorylation in response to H2O2.Proceedings of the National Academy of Sciences of the United States of America · 1997Article
- Characterization of two forms of protein kinase C alpha, with different substrate specificities, from skeletal muscle.The Biochemical journal · 1996Article
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5 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
The delta isoform of protein kinase C is phosphorylated on tyrosine in response to antigen activation of the high-affinity receptor for immunoglobulin E. While protein kinase C-delta associates with and phosphorylates this receptor, immunoprecipitation of the receptor revealed that little, if any, tyrosine-phosphorylated protein kinase C-delta is receptor associated. In vitro kinase assays with immunoprecipitated tyrosine-phosphorylated protein kinase C-delta showed that the modified enzyme had diminished activity toward the receptor gamma-chain peptide as a substrate but not toward histones or myelin basic protein peptide. We propose a model in which the tyrosine phosphorylation of protein kinase C-delta regulates the kinase specificity toward a given substrate. This may represent a general mechanism by which in vivo protein kinase activities are regulated in response to external stimuli.
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