Abstract
Membrane recruitment of SHIP is responsible for the inhibitory signal generated by FcγRIIB coligation to the BCR. By reducing the level of PIP3, SHIP regulates the association of the tyrosine kinase Btk with the membrane through PH domain–phosphoinositol lipid interactions. Inhibition of BCR signaling by either FcγRIIB coligation, membrane expression of SHIP, or inhibition of PI3K, conditions which result in decreased levels of PIP3, is suppressed by the expression of Btk as a membrane-associated chimera. Conversely, increasing PIP3 levels by deletion of SHIP results in increased Btk association with the membrane and hyperresponsive BCR signaling. These results suggest a central role for PIP3 in regulating the B cell stimulatory state by modulating Btk localization and thereby calcium fluxes.
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