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The pleckstrin homology domain of phospholipase C-.delta.1 binds with high affinity to phosphatidylinositol 4,5-bisphosphate in bilayer membranes
Abstract
The pleckstrin homology (PH) domain of phospholipase C-delta 1 (PLC-delta 1) binds to phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2) in phospholipid membranes with an affinity (Ka approximately 10(6) M-1) and specificity comparable to those of the native enzyme. PLC-delta 1 and its PH domain also bind inositol 1,4,5-trisphosphate, the polar head group of PI(4,5)P2, with comparable affinity and approximately 1:1 stoichiometry. A peptide corresponding to amino acids 30-43 of the PLC-delta 1 PH domain contains several basic residues predicted to bind PI(4,5)P2, but binds weakly and with little specificity for PI(4,5)P2; hence the tertiary structure of the isolated PH domain is required for high affinity PI(4,5)P2 binding. Our PI-(4,5)P2 binding results support the hypothesis that the intact PH domain, serving as a specific tether, directs PLC-delta 1 to membranes enriched in PI(4,5)P2 and permits the active site, located elsewhere in the protein, to hydrolyze multiple substrate molecules before this enzyme dissociates from the membrane surface.
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Metadata
- Authors
- Garcia, P., Gupta, R., Shah, S., Morris, A. J., Rudge, S. A., Scarlata, S., Petrova, V., McLaughlin, S., & Rebecchi, M. J.
- Venue
- Biochemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 1995-12-12
- Volume
- 34
- Issue
- 49
- Pages
- 16228-16234
- ISSN
- 0006-2960 (ISSN-L)
- 1520-4995
- OpenAlex
- W2082688327
- Cited by
- 289
- References
- 0
- FWCI
- 5.33
- Type
- journal article
- Language
- en
- Open access
- closed
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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