Abstract
Phospholipases are widely occurring and can be found in several different organisms, including bacteria, yeast, plants, animals, and viruses. Phospholipase C (PLC) is a class of phospholipases that cleaves phospholipids on the diacylglycerol (DAG) side of the phosphodiester bond producing DAGs and phosphomonoesters. Among PLCs, phosphoinositide-specific PLC (PI-PLC) constitutes an important step in the inositide signaling pathways. The structures of PI-PLC isozymes show conserved domains as well as regulatory specific domains. This is important, as most PI-PLCs share a common mechanism, but each of them has a peculiar role and can have a specific cell distribution that is linked to a specific function. More importantly, the regulation of PLC isozymes is fundamental in health and disease, as there are several PLC-dependent molecular mechanisms that are associated with the activation or inhibition of important physiopathological processes. Moreover, PI-PLC alternative splicing variants can play important roles in complex signaling networks, not only in cancer but also in other diseases. That is why PI-PLC isozymes are now considered as important molecules that are essential for better understanding the molecular mechanisms underlying both physiology and pathogenesis, and are also potential molecular targets useful for the development of innovative therapeutic strategies.
Highlights
Phospholipases are widely occurring and can be found in several different organisms, including bacteria, yeast, plants, animals, and viruses
Function phosphatidylcholine, even though it can act upon other lipids, such as phosphatidylethanolamine, giving rise to a class of nonspecific Phospholipase C (PLC) [1, 2]
Phosphoinositidespecific PLC (PI-PLC) enzymes utilize phosphoinositides as a specific substrate and their metabolism is implicated in a large series of signal transduction pathways
Summary
Phospholipases are widely occurring and can be found in several different organisms, including bacteria, yeast, plants, animals, and viruses. We shall point at the molecular features, function, regulation, and splicing variants of these enzymes and discuss their role in disease. The PH domain binds the heterotrimeric G␥ subunit in PI-PLC2 and PI-PLC3 isozymes [11], and mediates interactions with phosphatidylinositol-3,4,5-trisphosphate (PIP3) in PI-PLC␥1, where it is required for inducing a phosphoinositide 3-kinase (PI3K)-dependent translocation and activation [12].
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