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Site-specific O-glycosylation of members of the low-density lipoprotein receptor superfamily enhances ligand interactions
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Glycosylation within the LDLR ligand binding domain enhances the ligand binding affinity of the LDLR.
“Glycosylation (both N-linked and O-linked) within the ligand binding domain has been shown to enhance the ligand binding affinity of the LDLR [19–21].”
From Post-translational regulation of the low-density lipoprotein receptor provides new targets for cholesterol regulation (2024) · cites this paper as [19]
The title in the Additions and Corrections item (p. 8349) states that site-specific O-glycosylation of LDL receptor superfamily members enhances ligand interactions. The available text does not establish that glycosylation occurs within LDLR’s ligand-binding domain or that both N-linked and O-linked glycosylation increase LDLR ligand-binding affinity. (LLM, conf=0.78)
Experimental — accuracy not yet measuredThe ligand binding domain of LDLR has also been shown to be O-glycosylated.
“In addition to the glycosylated region near the transmembrane domain, the ligand binding domain of LDLR has also been shown to be O-glycosylated79,92.”
From Pathways and Molecular Mechanisms Governing LDL Receptor Regulation (2025) · cites this paper as [79]
The indexed copy is an Additions and Corrections notice (p. 8349), not the study’s substantive text. Its correction paragraph mentions LDLR assay controls but does not address O-glycosylation of the LDLR ligand-binding domain. Searches for that domain and O-glycosylation found no decisive passage in this copy. (LLM, conf=0.76)
Experimental — accuracy not yet measuredModification by O-glycosylation enhances binding of apolipoprotein ligands to LDLR, likely largely mediated by the GalNAc-transferase GalNAc-T1.
“Modification by O-glycosylation enhances binding of apolipoprotein ligands to LDLR, likely largely mediated by the GalNAc-transferase GalNaC-T1179,92.”
From Pathways and Molecular Mechanisms Governing LDL Receptor Regulation (2025) · cites this paper as [79]
Like other LDLR-related family members, following the ligand binding domain, the remaining extracellular portion of LDLR includes repeated EGF-like domains and YWTD repeats.
“Like other LDLR-related family members79, following the ligand binding domain, the remaining extracellular portion of the protein includes repeated epidermal-growth factor (EGF) like domains, and a series of tyrosine-tryptophan-threonine-asparagine repeats (YWTD repeats).”
From Pathways and Molecular Mechanisms Governing LDL Receptor Regulation (2025) · cites this paper as [79]
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Aldworth, H., & Hooper, N. M. (2024) · Biochemical Society Transactions · doi:10.1042/bst20230918 · Cited by 11
Metadata
- Authors
- Wang, S., Mao, Y., Narimatsu, Y., Ye, Z., Tian, W., Goth, C. K., Lira-Navarrete, E., Pedersen, N. B., Benito-Vicente, A., Martin, C., Uribe, K. B., Hurtado-Guerrero, R., Christoffersen, C., Seidah, N. G., Nielsen, R., Christensen, E. I., Hansen, L., Bennett, E. P., Vakhrushev, S. Y., Schjoldager, K. T., & Clausen, H.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2019-05
- Volume
- 294
- Issue
- 21
- Pages
- 8349
- ISSN
- 0021-9258
- Cited by
- 10
- References
- 0
- Language
- en
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