[HTML][HTML] Molecular basis of the recruitment of the SH2 domain-containing inositol 5-phosphatases SHIP1 and SHIP2 by FcγRIIB
P Bruhns, F Vély, O Malbec, WH Fridman… - Journal of Biological …, 2000 - ASBMB
FcγRIIB are single-chain low affinity receptors for IgG that negatively regulate
immunoreceptor tyrosine-based activation motif-dependent cell activation. They bear one
immunoreceptor tyrosine-based inhibition motif (ITIM) that becomes tyrosyl-phosphorylated
upon coaggregation of FcγRIIB with immunoreceptor tyrosine-based activation motif-bearing
receptors and that recruits SH2 domain-containing inositol 5-phosphatases (SHIPs) in vivo.
Synthetic FcγRIIB ITIM phosphopeptides, however, also bind SH2 domain-containing …
immunoreceptor tyrosine-based activation motif-dependent cell activation. They bear one
immunoreceptor tyrosine-based inhibition motif (ITIM) that becomes tyrosyl-phosphorylated
upon coaggregation of FcγRIIB with immunoreceptor tyrosine-based activation motif-bearing
receptors and that recruits SH2 domain-containing inositol 5-phosphatases (SHIPs) in vivo.
Synthetic FcγRIIB ITIM phosphopeptides, however, also bind SH2 domain-containing …