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*
Hospital de la Princesa, Madrid, Spain; and
Departament de Ciències Experimentals i de la Salut (Inmunología), Universitat Pompeu Fabra, Barcelona, Spain
The inhibitory receptor Ig-like transcript (ILT)2 (leukocyte
Ig-like receptor or CD85j) is a type I transmembrane protein expressed
by different leukocyte lineages. The extracellular region of ILT2 binds
HLA class I molecules, and its cytoplasmic domain displays four
immunoreceptor tyrosine-based inhibition motifs. Upon tyrosine
phosphorylation ILT2 recruits the Src homology 2 domain-containing
protein tyrosine phosphatase 1 (SHP-1) that is involved in negative
signaling. To address the structural basis of ILT2-mediated inhibitory
signaling, deletion and single tyrosine mutants were generated and
transfected in the COS-7 and rat basophilic leukemia cell lines; their
abilities to bind SHP-1 and to inhibit Fc
R-induced serotonin release
in rat basophilic leukemia cells were studied. Both biochemical and
functional analyses revealed tyrosines 644 (SIYATL) and 614
(VTYAQL) as the SHP-1 docking sites required for ILT2 inhibitory
function. Substitution of tyrosine 562 (VTYAEV) did not alter receptor
function. By contrast, mutation of tyrosine 533 (NLYAAV) interfered
with ILT2 tyrosine phosphorylation and the subsequent SHP-1
recruitment, thus supporting a regulatory role for this
motif.
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