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(Received for publication, July 9, 1996, and in revised form, August 14, 1996)
From the CD43, the most abundant membrane protein of T
lymphocytes, is able to initiate signal transduction pathways that lead
to Ca2+ mobilization and interleukin-2 production, yet the
molecular events involved in CD43's signal transduction pathway are
poorly understood. In the present report we show that activation of
both purified T lymphocytes and Jurkat cells, through CD43
cross-linking with the anti-CD43 L10 monoclonal antibody, induced CD43
association to Fyn kinase. This association is mediated by the Src
homology 3 (SH3) domain of Fyn, since a glutathione
S-transferase-Fyn SH3 fusion protein was able to
precipitate CD43 from lysates of CD43-activated T cells. A synthetic
peptide containing the SH3 binding sites of p85, located within the
amino acid sequence 300ERQPAPALPPKPPKP314, was
able to inhibit binding of CD43 to Fyn as well as to the glutathione
S-transferase-Fyn SH3 fusion protein. We also provide
evidence that upon CD43 cross-linking, Fyn is tyrosine-phosphorylated
in a time-dependent manner. Our results suggest that CD43
cross-linking on the T cell surface induces the interaction between
CD43 and Fyn, presumably through the Fyn SH3 domain and a putative SH3
binding site in CD43, leading to Fyn tyrosine phosphorylation and
signal propagation.
Volume 271, Number 44,
Issue of November 1, 1996
pp. 27564-27568
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
,
,
Instituto de
Biotecnología/Universidad Nacional Autónoma de Mexico,
Apartado Postal 510-3 Cuernavaca, Morelos 62250, México and the
§ Dana Farber Cancer Institute,
Boston, Massachusetts 02115
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