SAP is expressed endogenously in mouse splenic B cells and co-localizes and interacts with CD22. SAP binding to the inhibitory immunoreceptor CD22 regulates calcium mobilization in B cells.
Results suggest that CD22 is expressed on mouse primary T cells and capable of associating with the Src homology 2 domain-containing protein-tyrosine phosphatase SHP-1.
CD22 neither associates with nor functions in major histocompatibility complex (MHC) class II/Ig-alpha beta signaling and is actively excluded from cell surface MHC class II aggregates.
In the yeast two-hybrid system the carboxyl-terminal portion of the CD22 cytoplasmic tail encompassing tyrosine residues 843 and 863 is critical for binding of clathrin adaptor AP50 to CD22 an interaction required for internalization.
The expression and function of CD22 are differentially regulated in B-1 and conventional B-2 lymphocytes which are implicated in innate and adaptive immunity respectively.
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