Research ArticleImmunology

The autoinhibitory C-terminal SH2 domain of phospholipase C–γ2 stabilizes B cell receptor signalosome assembly

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Science Signaling  16 Sep 2014:
Vol. 7, Issue 343, pp. ra89
DOI: 10.1126/scisignal.2005392

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A Positive Role for an Autoinhibitory Domain in B Cell Signaling

Activation of B cells requires antigen-dependent stimulation of B cell receptors (BCRs), which become assembled into complexes that provide sustained signals. BCR stimulation causes the recruitment and activation of phospholipase C–γ2 (PLC-γ2), which results in Ca2+ mobilization. Although patients with the immune disorder PLAID have a variant PLC-γ2 that is devoid of an autoinhibitory domain, their B cells exhibit defective Ca2+ signaling and are dysregulated. Wang et al. found that B cells from PLAID patients failed to form stable BCR complexes and had defective activation of downstream effectors. Together, these data suggest that the autoinhibitory domain of PLC-γ2 is also required to stabilize clustered receptors for sustained signaling.