Regulation of phospholipase C-gamma2 networks in B lymphocytes.

The modulation of inositol-1,4,5-trisphosphate (IP3), a product of phospholipase C (PLC) activity, is one of a common signaling mechanism used in many biological systems. B lymphocytes also rely on IP3 and subsequent calcium signaling to ensure appropriate developmental outcomes, as well as antigen-specific responses. In establishing the optimal intensity and duration of the PLC-gamma activity, an important role has emerged for adaptor molecules, which direct the appropriate subcellular localization of PLC-gamma and induce its conformational changes. Generated IP3 binds to IP3 receptors located on the endoplasmic reticulum (ER), which in turn is essential for triggering calcium release from the ER and subsequent entry of extracellular calcium by so-called Ca2+ entry channels. Recent data has begun to shed new light on the connection between the calcium release and the influx of extracellular calcium, and the molecular identity of the Ca2+ entry channels.