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*
School of Pharmacy, University of Maryland, Baltimore, MD 21201; and
Boehringer Ingelheim Research and Development Center, Ridgefield, CT 06877
Lnk was originally cloned from a rat lymph node cDNA library and
shown to participate in T cell signaling. Human Lnk (hLnk) was cloned
by screening a Jurkat cell cDNA library. hLnk has a calculated
molecular mass of 63 kDa, and its deduced amino acid sequence indicates
the presence of an N-terminal proline-rich region, a pleckstrin
homology domain, and a Src homology 2 domain. When expressed in COS
cells, hLnk migrates with an apparent molecular mass of 75 kDa.
Confocal fluorescence microscope analysis indicates that in COS cells
transfected with an expression vector encoding a chimeric Lnk-green
fluorescent protein, hLnk is found at the juxtanuclear compartment and
also appears to be localized at the plasma membrane. Lnk is
tyrosine-phosphorylated by p56lck. Following
phosphorylation, p56lck binds to
tyrosine-phosphorylated hLnk through its Src homology 2 domain. In COS
cells cotransfected with hLnk, p56lck, and
CD8-
, hLnk associated with tyrosine-phosphorylated TCR -chain
through its Src homology 2 domain. The overexpression of Lnk in Jurkat
cells led to an inhibition of anti-CD3 mediated NF-AT-Luc
activation. Our study reveals a potentially new mechanism of T
cell-negative regulation.
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