Direct Interaction in T-cells between θPKC and the Tyrosine Kinase p59fyn
The protein kinase C (PKC) family has been clearly implicated in T-cell activation as have several nonreceptor protein-tyrosine kinases associated with the T-cell receptor, including p59fyn. This report demonstrates that θPKC and p59fyn specifically interact in vitro , in the yeast two-hybrid syste...
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Veröffentlicht in: | The Journal of biological chemistry 1999-07, Vol.274 (27), p.19003 |
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container_issue | 27 |
container_start_page | 19003 |
container_title | The Journal of biological chemistry |
container_volume | 274 |
creator | Dorit Ron Eugene W. Napolitano Anna Voronova Nicki J. Vasquez Doug N. Roberts Brenda L. Calio Roger H. Caothien Sherrie M. Pettiford Sarah Wellik Janis B. Mandac Lawrence M. Kauvar |
description | The protein kinase C (PKC) family has been clearly implicated in T-cell activation as have several nonreceptor protein-tyrosine
kinases associated with the T-cell receptor, including p59fyn. This report demonstrates that θPKC and p59fyn specifically
interact in vitro , in the yeast two-hybrid system, and in T-cells. Further indications of direct interaction are that p59fyn potentiates θPKC
catalytic activity and that θPKC is a substrate for tyrosine phosphorylation by p59fyn. This interaction may account for the
localization of θPKC following T-cell activation, pharmacological disruption of which results in specific cell-signaling defects.
The demonstration of a physical interaction between a PKC and a protein-tyrosine kinase expands the class of PKC-anchoring
proteins (receptors for activated C kinases (RACKs)) and demonstrates a direct connection between these two major T-cell-signaling
pathways. |
doi_str_mv | 10.1074/jbc.274.27.19003 |
format | Article |
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kinases associated with the T-cell receptor, including p59fyn. This report demonstrates that θPKC and p59fyn specifically
interact in vitro , in the yeast two-hybrid system, and in T-cells. Further indications of direct interaction are that p59fyn potentiates θPKC
catalytic activity and that θPKC is a substrate for tyrosine phosphorylation by p59fyn. This interaction may account for the
localization of θPKC following T-cell activation, pharmacological disruption of which results in specific cell-signaling defects.
The demonstration of a physical interaction between a PKC and a protein-tyrosine kinase expands the class of PKC-anchoring
proteins (receptors for activated C kinases (RACKs)) and demonstrates a direct connection between these two major T-cell-signaling
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kinases associated with the T-cell receptor, including p59fyn. This report demonstrates that θPKC and p59fyn specifically
interact in vitro , in the yeast two-hybrid system, and in T-cells. Further indications of direct interaction are that p59fyn potentiates θPKC
catalytic activity and that θPKC is a substrate for tyrosine phosphorylation by p59fyn. This interaction may account for the
localization of θPKC following T-cell activation, pharmacological disruption of which results in specific cell-signaling defects.
The demonstration of a physical interaction between a PKC and a protein-tyrosine kinase expands the class of PKC-anchoring
proteins (receptors for activated C kinases (RACKs)) and demonstrates a direct connection between these two major T-cell-signaling
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kinases associated with the T-cell receptor, including p59fyn. This report demonstrates that θPKC and p59fyn specifically
interact in vitro , in the yeast two-hybrid system, and in T-cells. Further indications of direct interaction are that p59fyn potentiates θPKC
catalytic activity and that θPKC is a substrate for tyrosine phosphorylation by p59fyn. This interaction may account for the
localization of θPKC following T-cell activation, pharmacological disruption of which results in specific cell-signaling defects.
The demonstration of a physical interaction between a PKC and a protein-tyrosine kinase expands the class of PKC-anchoring
proteins (receptors for activated C kinases (RACKs)) and demonstrates a direct connection between these two major T-cell-signaling
pathways.</abstract><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>10383400</pmid><doi>10.1074/jbc.274.27.19003</doi></addata></record> |
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title | Direct Interaction in T-cells between θPKC and the Tyrosine Kinase p59fyn |
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