Abstract
Immunoglobulin (Ig)-like transcripts (ILT) receptors, also known as monocyte/macrophage Ig-like receptors (MIRs) or leukocyte Ig-like receptors (LIRs)[1, 2], constitute a family of receptors which belong to the immunoglobulin superfamily. They are characterized by either 2 or 4 homologous extracellular C-2 type Ig-like domains or by different transmembrane and cytoplasmic domains. One subset of ILT receptors (ILT2, ILT3, ILT4, ILT5 and LIRE) displays long cytoplasmic tails containing immunoreceptor tyrosine-based inhibitory motifs (ITIMs) and delivers inhibitory signals by recruiting SHP-1 protein tyrosine phosphatase [3–5]. A second subset of ILT receptors (ILT1, ILT7, ILT8 and LIR6) is characterized by the presence of a positively charged amino acid residue within the transmembrane region and by a short cytoplasmic tail with no obvious signal transduction motifs. These receptors mediate cell activation by associating with the gamma chain of Fc receptors (FcR’y) [6]. FcR’y recruits protein tyrosine kinases through a cytoplasmic immunoreceptor tyrosine-based activation motif (1TAM).
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Cella, M., Nakajima, H., Facchetti, F., Hoffmann, T., Colonna, M. (2000). ILT Receptors at the Interface Between Lymphoid and Myeloid Cells. In: Melchers, F. (eds) Lymphoid Organogenesis. Current Topics in Microbiology and Immunology, vol 251. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-57276-0_20
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DOI: https://doi.org/10.1007/978-3-642-57276-0_20
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