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Analysis of CD36 Binding Domains: Ligand Specificity Controlled by Dephosphorylation of an Ectodomain

Analysis of CD36 Binding Domains: Ligand Specificity Controlled by Dephosphorylation of an Ectodomain,10.1126/science.7504322,Science,Adam S. Asch,Isa

Analysis of CD36 Binding Domains: Ligand Specificity Controlled by Dephosphorylation of an Ectodomain   (Citations: 73)
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The protein CD36 is a membrane receptor for thrombospondin (TSP), malaria-infected erythrocytes, and collagen. Three functional sequences were identified within a single disulfide loop of CD36: one that mediates TSP binding (amino acids 87 to 99) and two that support malarial cytoadhesion (amino acids 8 to 21 and 97 to 110). One of these peptides (p87-99) is a consensus protein kinase C (PKC) phosphorylation site. Dephosphorylation of constitutively phosphorylated CD36 in resting platelets and a megakaryocytic cell line led to the loss of collagen adhesion and platelet reactivity to collagen, with a reciprocal increase in TSP binding. PKC-mediated phosphorylation of this ectodomain resulted in a loss of TSP binding and the reciprocal acquisition of collagen binding. In site-directed mutagenesis studies, when the threonine phosphorylation site was changed to alanine, CD36 was expressed in a dephosphorylated state and bound to TSP constitutively.
Journal: Science , vol. 262, no. 5138, pp. 1436-1440, 1993
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