Aggregation of many cell surface receptors results in tyrosine phosphorylation of intracellular proteins. The phosphorylation state of these proteins then controls enzymatic activity and protein-protein association or dissociation thereby propagating and regulating downstream signal transduction. The level of protein phosphorylation of a molecule is due to the balance between protein tyrosine kinase and phosphatase activities. Therefore, it is important to understand the role of the protein tyrosine phosphatases in initiating, maintaining and regulating signal transduction in cells. In studies during this last year we found that the SH2 domain containing protein tyrosine phosphatase SHP-1 and SHP-2 associate with FceRI and that the SHP-2 also associates with the adhesion molecule PECAM-1 that is tyrosine phosphorylated by activation of different integrin or immune receptors.

Agency
National Institute of Health (NIH)
Institute
National Institute of Dental & Craniofacial Research (NIDCR)
Type
Intramural Research (Z01)
Project #
1Z01DE000644-04
Application #
6104659
Study Section
Special Emphasis Panel (OIIB)
Project Start
Project End
Budget Start
Budget End
Support Year
4
Fiscal Year
1998
Total Cost
Indirect Cost
Name
National Institute of Dental & Craniofacial Research
Department
Type
DUNS #
City
State
Country
United States
Zip Code