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Blood, 1 February 2002, Vol. 99, No. 3, pp. 957-965
IMMUNOBIOLOGY
Molecular dissection of the signaling and costimulatory functions
of CD150 (SLAM): CD150/SAP binding and CD150-mediated costimulation
Duncan Howie,
María Simarro,
Joan Sayos,
Maria Guirado,
Jaime Sancho, and
Cox Terhorst
From the Division of Immunology, Beth Israel Deaconess
Medical Center, Harvard Medical School, Boston, Massachusetts;
Departament de Ciencias Experimentals i de la Salut Laboratori de
Immunologia, Universitat Pompeu Fabra Barcelona, Spain; and Instituto
de Parasitología y Biomedicina, Consejo Superior de
Investigaciones Científicas, Granada, Spain.
CD150 signaling lymphocytic activation molecule (SLAM), a
T/B/dendritic cell surface glycoprotein, is a costimulatory receptor involved in T-cell activation and is also a receptor for measles virus.
CD150-induced signal transduction is controlled by
SAP/SH2D1A, the gene that is aberrant in X-linked
lymphoproliferative disease and familial hemophagocytic
lymphohistiocytosis. This report shows that CD150 colocalizes with the
T-cell receptor (TCR) following CD3 triggering in human peripheral
blood T cells and is rapidly and reversibly tyrosine phosphorylated on
TCR cross-linking. The Src-like kinases Lck and Fyn phosphorylate
tyrosine residues in the cytoplasmic tail of CD150. The results
demonstrate that the SAP protein has 2 modes of binding to CD150.
Binding to the motif Thr-Ile-Tyr281Ala-Gln-Val occurs in a
phosphotyrosine-independent fashion and to the motif
Thr-Val-Tyr327Ala-Ser-Val in a phosphotyrosine-dependent manner. Within
both SAP binding motifs the threonine residue at position  2 to
tyrosine is essential to stabilize the interaction irrespective of
tyrosine phosphorylation, a feature unique to the SAP SH2 domain. A
leucine residue, Leu278, further stabilizes nonphospho binding of SAP
to Tyr281 of CD150. SAP blocking of the tyrosine phosphatase SHP-2
occurs primarily on Tyr281 of CD150 because SHP-2 requires both Tyr281
and Tyr327 for binding to CD150, and SAP binds to nonphosphorylated
Tyr281. CD150 exhibits lateral mobility, segregating into intercellular
contacts. The lateral mobility and homophilic clustering of CD150
between neighboring cells is not dependent on SAP/CD150 interaction.
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