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Updated: May 17, 2025

PIP-on-a-chip: A Label-free Study of Protein-phosphoinositide Interactions
Published on: July 27, 2017
Phosphoinositide-specific phospholipase C enzymes: Recent advances in a long journey
Calum Macrae1, Damjan Lalović1, Tom D Bunney1
1Institute of Structural and Molecular Biology, Division of Biosciences, University College London, Gower St, London, WC1E 6BT, UK.
Abstract:
A journey that started with the discovery of phospholipase C catalysed inositol-lipid hydrolysis as a receptor-controlled signalling event, culminated in defining molecular properties and roles of phosphoinositide-specific phospholipase C (PLC) families. Currently, there are six classical (13 isoforms) and one atypical (3 isoforms) family, expressed in a wide range of mammalian cells where they perform key functions in intracellular signal transduction. We here highlight recent advances in the PLC field, mostly resulting from studies of the PLCγ family members, PLCγ1 and PLCγ2. These new discoveries include elucidation of their structural and functional properties as well as their roles in physiology and disease development. We also illustrate the involvement of classical PLC families in control of cellular processes mediated not only by the PtdIns(4,5)P2-derived second messengers, resulting from the PLC hydrolysis, but also by second messenger-independent consequences of PtdIns(4,5)P2 hydrolysis. Presented examples are focused on regulation of ion channels by PtdIns(4,5)P2.
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