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Cutting Edge |
Immunology Program, Sloan-Kettering Institute for Cancer Research, Memorial Sloan-Kettering Cancer Center, New York, NY 10021
Inhibitory NK receptors with ligand specificity for MHC class I
recruit Src homology 2-containing protein tyrosine phosphatase-1
(SHP-1) phosphatase and prevent autocytotoxicity. Activation of SHP-1
depends upon Src kinase-mediated tyrosine
phosphorylation of the cytoplasmic domain of the
inhibitory receptor. In this study we demonstrate, by quantitative
temporal analysis, that talin, Lck, and SHP-1 are recruited to
the synapse within 1 min in both cytolytic and noncytolytic conjugates.
Polarization of talin and Lck rapidly disappears in the noncytolytic
interactions but persists in cytolytic interactions, where protein
kinase C-
, Src homology 2 domain-containing leukocyte protein of 76
kDa, and lysosomes are recruited within 5 min. At 1 min SHP-1
clusters in the periphery of the cytolytic synapse, whereas it clusters
in the center of the noncytolytic synapse. Lck has multifocal
distribution in both synapses consistent with the shared requirement
for early tyrosine phosphorylation. Our studies
indicate that the spatial location of SHP-1 in the synapse
distinguishes noncytolytic from cytolytic interactions within the first
minute.
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