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CUTTING EDGE |
2 Src Homology 2 Domains with BLNK Is Critical for B Cell Antigen Receptor Signaling1
*
Department of Molecular Genetics, Institute for Liver Research, Kansai Medical University, Moriguchi, Japan; and
Department of Integrated Medicine, Omiya Medical Center, Jichi Medical School, Omiya, Japan
To explore the mechanism(s) by which phospholipase C (PLC)-
2
participates in B cell Ag receptor (BCR) signaling, we have studied the
function of PLC-2 mutants in B cells deficient in PLC-2. Mutation
of the N-terminal Src homology 2 domain [SH2(N)] resulted in the
complete loss of inositol 1,4,5-trisphosphate generation upon BCR
engagement. A possible explanation for the SH2(N) requirement was
provided by findings that this mutation abrogates the association of
PLC-2 with an adaptor protein BLNK. Moreover, expression of a
membrane-associated form (CD16/PLC-2) with SH2(N) mutation required
coligation of BCR and CD16 for inositol 1,4,5-trisphosphate generation.
Together, our results suggest a central role for the SH2(N) domain in
directing PLC-2 into the close proximity of BCR signaling complex by
its association with BLNK, whereby PLC-2 becomes tyrosine
phosphorylated and thereby
activated.
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