Phospholipid Binding Properties and Functional Characterization of a Sea Urchin Phospholipase Cdelta in Urchin and Mouse Eggs.
From: Department of Pharmacology, University of Oxford, Oxford OX1 3QT, UK.
Biochemical and biophysical research communications
- Publish Date: Jun 2007
- ISSN: 0006-291X
- Volume: 357
- Issue: 4
- Pages: 964-70
- Medium: Print
- Language: English
- Citation (JAMA): Coward Kevin, Owen Helen, Tunwell Richard, et al. Phospholipid Binding Properties and Functional Characterization of a Sea Urchin Phospholipase Cdelta in Urchin and Mouse Eggs.. Biochem. Biophys. Res. Commun. Jun 2007;357:964-70
Abstract
We recently identified a novel phospholipase Cdelta isoform, PLC-deltasu, in sea urchin gametes, whose precise functional role during fertilization and early embryogenesis remains unknown. Here, we characterized the binding of the PLC-deltasu PH domain to different phosphatidylinositol (PI) phospholipids and studied changes in its localization during fertilization. The PLC-deltasu PH domain bound most strongly to PI(3,4)P(2) and PI(3,5)P(2) phospholipids, in contrast to the PLCdelta1 PH domain which bound predominantly to PI(4,5)P(2). A green fluorescent protein tagged PLC-deltasu PH domain localized to the plasma membrane and its localization increased at fertilization and following addition of a Ca(2+) ionophore. However, recombinant PLC-deltasu failed to cause Ca(2+) signals like those seen at fertilization, in mouse and sea urchin eggs. Our findings suggest that PLC-deltasu is unlikely to be directly involved in the process of egg activation but may play a role in mediating extracellular signals transmitted via the PI 3’-kinase pathway.
Mesh Headings (Keywords): Animals, Cells, Cultured, Embryonic Development, Fertilization, Isoenzymes, Mice, Phospholipase C delta, Phospholipids, Protein Binding, Sea Urchins, Type C Phospholipases, Zygote
Check for Full Text / PubMed Unique Identifier (PMID): 17466265
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