作者: Damiana Alvarez-Errico , Helena Aguilar , Friederike Kitzig , Tamara Brckalo , Joan Sayós
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摘要: Using a three-hybrid strategy, we have identified novel cell surface molecule which interacts with the Src homology 2 (SH2) domains of SH2 domain-containing protein tyrosine phosphatase 1 (SHP-1), termed "immune receptor expressed on myeloid cells 1" (IREM-1). The full-length cDNA coding for polypeptide 290 amino acids presents an extracellular single V-type Ig domain, transmembrane region and cytoplasmic tail five residues, two are in context immunoreceptor tyrosine-based inhibitory motif. Moreover, encoding three other splicing forms IREM-1, named IREM-1 splice variant (Sv)1, Sv2 Sv3 were cloned by reverse transcription (RT)-PCR. gene contains nine exons, is located human chromosome 17 (17q25.1) homologous to previously molecules CMRF-35 IRp60. RT-PCR, northern blot FACS analysis specific monoclonal antibodies indicated that monocytes, granulocytes, leukemia lines. Western confirmed recruitment SHP-1 demonstrated phosphotyrosine residue 205 main docking site this interaction. Finally, cross-linking results inhibition FcRepsilon-induced activation. Our indicate superfamily cells.