ArticlebioRxiv : the preprint server for biology2026
PLCβs are recruited to the plasma membrane in macrophages by both Gβγ and Gα
Article in bioRxiv : the preprint server for biology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
PLCβ enzymes cleave PIP2 from the plasma membrane, producing IP3 and DAG, which regulate intracellular Ca Significance Statement: PLCβ enzymes are critical mediators of signal transduction with roles in neuronal, cardiac, and immunological signaling. Despite this importance, many aspects of their function and regulation remain poorly understood. PLCβs are aqueous soluble but must partition onto the membrane surface to access their lipid substrate, which enables regulation at the partitioning step, the catalytic step, or both. We previously demonstrated that membrane recruitment and orientation of the catalytic core on the membrane surface underlie the PLCβ regulation by one effector, Gβγ. Using macrophages as a model system for physiological signaling, we demonstrate that Gβγ is capable of independently activating PLCβ via membrane recruitment under the conditions of endogenous signaling.
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