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Characterization of low density lipoprotein receptor ligand interactions by fluorescence resonance energy transfer
Abstract
The low density lipoprotein receptor (LDLR) is the prototype of a family of cell surface receptors involved in a wide range of biological processes. A soluble low density lipoprotein receptor (sLDLR) and a tryptophan (Trp)-deficient variant human apolipoprotein E3 (apoE3) N-terminal domain (NT) were used in binding studies. The sole cysteine in apoE3-NT was covalently modified with an extrinsic fluorescence probe, N-(iodoacetyl)-N'-(5-sulfo-1-napthyl)ethylenediamine (AEDANS), and the protein was complexed with lipid. Incubation of sLDLR with AEDANS-Trp-null apoE3-NT dimyristoylphosphatidylcholine (DMPC) disks, but not lipid-free AEDANS-apoE, induced an enhancement in AEDANS fluorescence emission intensity (excitation, 280 nm) consistent with intermolecular energy transfer from excited Trp in sLDLR to receptor-bound apoE. Ligand binding to sLDLR required calcium and was saturable. In competition binding assays, unlabeled apoE3-NT DMPC inhibited AEDANS-apoE DMPC binding to sLDLR more effectively than low density lipoprotein. Fluorescence changes in this system reflected pH-dependent ligand binding and release from sLDLR consistent with models derived from the X-ray crystal structure of the receptor at endosomal pH. Intermolecular energy transfer from excited Trp in LDLR family members to fluorescently tagged ligands represents a sensitive and convenient assay for the characterization of the myriad molecular interactions ascribed to this family of receptor.
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The EGF-like and YWTD repeats are thought to allow proper positioning of the ligand binding domain and have been shown to promote release of cargo in the endosome in a pH-dependent manner.
“These repeats are thought to both allow proper positioning of the ligand binding domain and have been shown to promote the release of cargo in the endosome in a pH-dependent manner80.”
From Pathways and Molecular Mechanisms Governing LDL Receptor Regulation (2025) · cites this paper as [80]
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Pathways and Molecular Mechanisms Governing LDL Receptor Regulation
Schmidt, H. M., Jarrett, K. E., de Aguiar Vallim, T. Q., & Tarling, E. J. (2025) · Circulation Research · doi:10.1161/circresaha.124.323578 · Cited by 33
Metadata
- Authors
- Yamamoto, T., Lamoureux, J., & Ryan, R. O.
- Venue
- Journal of Lipid Research
- Publisher
- Elsevier BV
- Published
- 2006-05
- Volume
- 47
- Issue
- 5
- Pages
- 1091-1096
- ISSN
- 0022-2275
- Cited by
- 15
- References
- 4
- Language
- en
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