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• W2893773596 endingPage "17490" @default.
• W2893773596 startingPage "17477" @default.
• W2893773596 abstract "Phospholipase C (PLC) enzymes produce second messengers that increase the intracellular Ca2+ concentration and activate protein kinase C (PKC). These enzymes also share a highly conserved arrangement of core domains. However, the contributions of the individual domains to regulation are poorly understood, particularly in isoforms lacking high-resolution information, such as PLCɛ. Here, we used small-angle X-ray scattering (SAXS), EM, and functional assays to gain insights into the molecular architecture of PLCɛ, revealing that its PH domain is conformationally dynamic and essential for activity. We further demonstrate that the PH domain of PLCβ exhibits similar dynamics in solution that are substantially different from its conformation observed in multiple previously reported crystal structures. We propose that this conformational heterogeneity contributes to subfamily-specific differences in activity and regulation by extracellular signals. Phospholipase C (PLC) enzymes produce second messengers that increase the intracellular Ca2+ concentration and activate protein kinase C (PKC). These enzymes also share a highly conserved arrangement of core domains. However, the contributions of the individual domains to regulation are poorly understood, particularly in isoforms lacking high-resolution information, such as PLCɛ. Here, we used small-angle X-ray scattering (SAXS), EM, and functional assays to gain insights into the molecular architecture of PLCɛ, revealing that its PH domain is conformationally dynamic and essential for activity. We further demonstrate that the PH domain of PLCβ exhibits similar dynamics in solution that are substantially different from its conformation observed in multiple previously reported crystal structures. We propose that this conformational heterogeneity contributes to subfamily-specific differences in activity and regulation by extracellular signals." @default.
• W2893773596 created "2018-10-05" @default.
• W2893773596 creator A5009590524 @default.
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• W2893773596 creator A5091146367 @default.
• W2893773596 date "2018-11-01" @default.
• W2893773596 modified "2023-10-16" @default.
• W2893773596 title "Direct observation of conformational dynamics of the PH domain in phospholipases Cɛ and β may contribute to subfamily-specific roles in regulation" @default.
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• W2893773596 doi "https://doi.org/10.1074/jbc.ra118.003656" @default.
• W2893773596 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6231117" @default.
• W2893773596 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/30242131" @default.
• W2893773596 hasPublicationYear "2018" @default.
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