Structure/Function Relationships of Phospholipases C Beta

Title:Structure/Function Relationships of Phospholipases C Beta

Volume: 14 Issue: 8

Author(s): Massimo Sandal, Daniele Paltrinieri, Paolo Carloni, Francesco Musiani and Alejandro Giorgetti

Affiliation:

Keywords: Phospholipases C beta, cell signaling, protein structural biology.

Abstract: 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 G_q family (Gα_q), the Gβγ subunits released by the inhibitory G-protein (G_i) 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 Gα_q. 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.

Cite this article as:

Sandal Massimo, Paltrinieri Daniele, Carloni Paolo, Musiani Francesco and Giorgetti Alejandro, Structure/Function Relationships of Phospholipases C Beta, Current Protein & Peptide Science 2013; 14 (8) . https://dx.doi.org/10.2174/13892037113146660085