Structure/Function Relationships of Phospholipases C Beta
Massimo Sandal, Daniele Paltrinieri, Paolo Carloni, Francesco Musiani and Alejandro Giorgetti
Affiliation: Department of Biotechnology, University of Verona, Ca' Vignal 1: strada le Grazie 15, I-37134 Verona, Italy.
Keywords: Phospholipases C beta, cell signaling, protein structural biology.
Phospholipases C beta (PLC-βs) are essential components of the signal transduction of metazoans. They catalyze
the production of the second messengers inositol-1,4,5-trisphosphate (IP3) and diacylglycerol (DAG) from the hydrolysis
of phosphatidylinositol-4,5-bisphosphate (PIP2). These enzymes are activated by G-protein-coupled receptors
(GPCRs) through the interaction with the alpha subunit of heterotrimeric G-proteins belonging to the Gq family (Gαq), the
Gβγ subunits released by the inhibitory G-protein (Gi) and Ca2+ ions. Here we review current structural insights on these
important proteins, with a particular focus on the most structurally characterized isoform (PLC-β3) and the activation
mechanism operated by Gαq. We propose, following the lead of recent studies, that a tight combination of experiments
and molecular simulations are instrumental in further enlightening the structure/function understanding of PLC-βs.
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