Title : Role of the Syk autophosphorylation site and SH2 domains in B cell antigen receptor signaling.

Pub. Date : 1995 Dec 1

PMID : 7500027






5 Functional Relationships(s)
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1 A possible explanation for this requirement was provided by findings that recruitment of Syk to tyrosine-phosphorylated immunoglobulin (Ig) alpha and Ig beta requires both Syk SH2 domains. Tyrosine spleen tyrosine kinase Mus musculus
2 A possible explanation for this requirement was provided by findings that recruitment of Syk to tyrosine-phosphorylated immunoglobulin (Ig) alpha and Ig beta requires both Syk SH2 domains. Tyrosine spleen tyrosine kinase Mus musculus
3 A Syk mutant in which the putative autophosphorylation site (Y518/Y519) of Syk was changed to phenylalanine was also defective in signal transduction; however, this mutation did not affect recruitment to the phosphorylated immunoreceptor family tyrosine-based activation motifs (ITAMs). Tyrosine spleen tyrosine kinase Mus musculus
4 A Syk mutant in which the putative autophosphorylation site (Y518/Y519) of Syk was changed to phenylalanine was also defective in signal transduction; however, this mutation did not affect recruitment to the phosphorylated immunoreceptor family tyrosine-based activation motifs (ITAMs). Tyrosine spleen tyrosine kinase Mus musculus
5 These findings not only confirm that both SH2 domains are necessary for Syk binding to tyrosine-phosphorylated Ig alpha and Ig beta but indicate that this binding is necessary for Syk (Y518/519) phosphorylation after BCR ligation. Tyrosine spleen tyrosine kinase Mus musculus