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•] describe the cloning and initial characterization of SLP-65/BLNK/BASH in B cells. Fu et al. isolated SLP-65 from BCR-activated human Ramos B cells based on its ability to bind PLCγ1, whereas Goitsuka et al. utilized PCR-based subtraction and differential hybridization to isolate a cDNA preferentially expressed in chicken B cells of the bursa of Fabricius. Both groups show that SLP-65 is tyrosine phosphorylated by Syk upon BCR stimulation. Fu et al. show that SLP-65 associates with PLCγ, Vav, Grb2 and Nck, but not Shc, in a B cell line. However, Goitsuka et al. find an association between SLP-65 and Shc. Fu et al. also show that overexpression of SLP-65 in B cells augments BCR-induced PLCγ1/γ2 phosphorylation and NF-AT activation, and that mutation of four of its tyrosine residues results in decreased NF-AT activation compared with parental cells. In contrast, Goitsuka et al.
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•] describe the cloning and initial characterization of SLP-65/BLNK/BASH in B cells. Fu et al. isolated SLP-65 from BCR-activated human Ramos B cells based on its ability to bind PLCγ1, whereas Goitsuka et al. utilized PCR-based subtraction and differential hybridization to isolate a cDNA preferentially expressed in chicken B cells of the bursa of Fabricius. Both groups show that SLP-65 is tyrosine phosphorylated by Syk upon BCR stimulation. Fu et al. show that SLP-65 associates with PLCγ, Vav, Grb2 and Nck, but not Shc, in a B cell line. However, Goitsuka et al. find an association between SLP-65 and Shc. Fu et al. also show that overexpression of SLP-65 in B cells augments BCR-induced PLCγ1/γ2 phosphorylation and NF-AT activation, and that mutation of four of its tyrosine residues results in decreased NF-AT activation compared with parental cells. In contrast, Goitsuka et al. find that overexpression of SLP-65 interferes with BCR-induced NF-AT activation.
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3 generation. These defects can be overcome by transfection of either wild-type BLNK or a membrane-bound form of PLCγ2. In addition BCR-stimulated JNK and p38 activation were abrogated in this mutant cell line and could not be restored by expression of a membrane-bound form of PLCγ2, suggesting that BLNK is also involved in the Rac1/JNK pathway.
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3 generation. These defects can be overcome by transfection of either wild-type BLNK or a membrane-bound form of PLCγ2. In addition BCR-stimulated JNK and p38 activation were abrogated in this mutant cell line and could not be restored by expression of a membrane-bound form of PLCγ2, suggesting that BLNK is also involved in the Rac1/JNK pathway.
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