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(Received for publication, May 27, 1997)
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From the Activation of the cellular Src tyrosine kinase
depends upon dephosphorylation of the carboxyl-terminal inhibitory
tyrosine phosphorylation site. Herein we show that Src isolated from
human platelets and Jurkat T cells is preferentially dephosphorylated at its inhibitory phosphotyrosine site by the SHP-1 tyrosine
phosphatase. The data also revealed association of Src with SHP-1 in
both platelets and lymphocytes and the capacity of Src to phosphorylate
SHP-1 and interact with the SHP-1 NH2-terminal SH2
domain in vitro. Analysis of Src activity in thymocytes
from SHP-1-deficient motheaten and viable motheaten mice revealed this
kinase activity to be substantially lower than that detected in
wild-type thymocytes, but to be enhanced by in vitro
exposure to SHP-1. Similarly, immunoblotting analysis of thymocyte Src
expression before and after selective depletion of active Src protein
indicated that the proportion of active relative to inactive Src
protein is markedly reduced in motheaten compared with wild-type cells.
These observations, together with the finding of reduced Src activity
in HEY cells expressing a dominant negative form of SHP-1, provide
compelling evidence that SHP-1 functions include the positive
regulation of Src activation.
Departments of Medicine, Immunology and
Medical Genetics and Microbiology, University of Toronto and the Samuel
Lunenfeld Research Institute, Mount Sinai Hospital, Toronto, Ontario
M5G 1X5, Canada, the Department of Molecular Oncology, M.D.
Anderson Cancer Center, Houston, Texas 77030, and the
Toronto Hospital Research Institute and the
Canadian Red Cross Society, Toronto, Ontario M5G 2M1, Canada
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