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J. Biol. Chem., Vol. 276, Issue 49, 45654-45661, December 7, 2001
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,
From the Laboratory of Lymphocyte Biology, NHLBI, National
Institutes of Health, Bethesda, Maryland 20892
In addition to engagement of the T cell
receptor-CD3 complex, T lymphocytes can be activated by a variety of
cell surface molecules including the ~50-kDa surface receptor CD2.
While the majority of biochemical signaling elements are triggered by
either CD2 or TcR-CD3 receptors, a small number of proteins are engaged by only one receptor. Recently, p62dok (Dok1), a member of the
Dok family of adapter molecules, has been reported to be activated by
CD2 and not by CD3 engagement. Here we have examined the role of
p62dok in CD2-dependent signaling in Jurkat T
cells. As previously reported, we find that ligation of the CD2
molecule by mitogenic pairs of anti-CD2 mAbs led to phosphorylation of
p62dok. While CD2-induced p62dok tyrosine
phosphorylation was independent of both the p36/38 membrane adapter
protein linker of activated T cells (LAT) and the ZAP70/Syk family of kinases, it was dependent upon the Src family of kinases including Lck and Fyn. We find further that CD2 engagement induced the
association of tyrosine-phosphorylated p62dok to Crk-L. The
CD2-dependent association of p62dok to Crk-L was
independent of expression of the ZAP70/Syk family of kinases. Of note,
while T cell receptor-CD3 engagement did not induce either
p62dok phosphorylation or Crk-L association in Jurkat T cells,
it did inhibit CD2-dependent p62dok-Crk-L
complexes; this TcR-CD3-mediated regulation was dependent upon ZAP70
kinase activity. Our data suggest that phosphorylation of
p62dok and its interaction with other signaling proteins may
depend upon integrated signals emanating from the CD2 receptor,
utilizing a ZAP70/LAT-independent pathway, and the TcR-CD3 receptor,
which is ZAP70/Syk-dependent.
Supported by a fellowship from Fondazione, "Istituto
Pasteur-Fondazione Cenci-Bolognetti," University of Rome "La
Sapienza," Italy.
§
To whom correspondence should be addressed: NHLBI, Bldg. 10, Rm.
6C208, 10 Center Dr., Bethesda, MD 20892. Tel.: 301-402-6786; Fax:
301-480-1792; E-mail: biererb@nih.gov.
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