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A TIRF Microscopy Technique for Real-time, Simultaneous Imaging of the TCR and its Associated Signaling Proteins
Published on: March 22, 2012
Direct interaction in T-cells between thetaPKC and the tyrosine kinase p59fyn
D Ron1, E W Napolitano, A Voronova
1Telik, Inc., South San Francisco, California 94080, USA.
The Journal of Biological Chemistry
|June 26, 1999
Summary
Protein kinase C (PKC) interacts with p59fyn, a protein-tyrosine kinase, during T-cell activation. This physical interaction influences T-cell signaling and localization, revealing a direct link between these pathways.
Area of Science:
- Immunology
- Cell Biology
- Biochemistry
Background:
- Protein kinase C (PKC) family members are crucial for T-cell activation.
- Nonreceptor protein-tyrosine kinases, such as p59fyn, are associated with the T-cell receptor and involved in T-cell signaling.
Purpose of the Study:
- To investigate the physical interaction between thetaPKC and p59fyn.
- To elucidate the functional consequences of this interaction in T-cells.
Main Methods:
- In vitro binding assays
- Yeast two-hybrid system
- Analysis of T-cells
Main Results:
- ThetaPKC and p59fyn demonstrate specific interaction in vitro, yeast, and T-cells.
- p59fyn enhances thetaPKC catalytic activity.
- ThetaPKC serves as a substrate for tyrosine phosphorylation by p59fyn.
Conclusions:
- A direct physical interaction exists between thetaPKC and p59fyn.
- This interaction is significant for thetaPKC localization and T-cell signaling.
- The findings expand the known RACKs and link PKC and protein-tyrosine kinase signaling pathways in T-cells.
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