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J Biol Chem, Vol. 273, Issue 23, 14218-14224, June 5, 1998
From the CD43, the most abundant membrane
protein of T lymphocytes, is able to initiate signals that lead to
Ca2+ mobilization and interleukin-2 production, yet
the molecular events involved in signal transduction pathway of the
CD43 molecule are only beginning to be understood. We have shown
recently that cross-linking CD43 on the cell surface of human T
lymphocytes with the anti-CD43 monoclonal antibody L10 leads to
CD43-Fyn kinase interactions and to Fyn phosphorylation on tyrosine
residues. This interaction seems to be mediated by the SH3 domain of
Fyn and a proline-rich sequence located in the cytoplasmic domain of
CD43. Here we show that CD43-specific activation of human T lymphocytes
induced tyrosine phosphorylation of the adaptor protein Shc and of the
guanine exchange factor Vav, as well as the formation of a
macromolecular complex that comprises Shc, GRB2, and Vav. CD43 ligation
resulted in enhanced formation of Vav·SLP-76 complexes and in the
activation and nuclear translocation of ERK2. Cross-linking of the CD43
molecule in 3T3-CD43+ cells induced luciferase activity
from a construct under the control of the Fos serum responsive element.
Altogether, these data suggest that the mitogen-activated protein
kinase pathway is involved in CD43-dependent interleukin-2
gene expression.
T Cell Activation through the CD43 Molecule Leads to Vav
Tyrosine Phosphorylation and Mitogen-activated Protein Kinase
Pathway Activation
,,
Instituto de Biotecnología/UNAM,
APDO. Postal 510-3 Cuernavaca, Morelos, 62250, México and the
§ Dana Farber Cancer Institute and the Department of
Pediatrics, Harvard Medical School,
Boston, Massachusetts 02115
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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