The DOI matches its Crossref record; 65 of the 68 references it cites were found in a registry or an index.
Transferrin receptor internalization sequence YXRF implicates a tight turn as the structural recognition motif for endocytosis
Abstract
Using detailed functional studies on 24 human transferrin receptor mutants, we identified YXRF as the internalization sequence. Provided that at least 7 residues separate this tetrapeptide from the transmembrane region, changing the tetrapeptide position within the TR cytoplasmic domain does not reduce internalization activity. Thus, any conformational determinant for internalization must be localized to the YXRF sequence. Twenty-eight tetrapeptide analogs of YXRF, found by an unbiased search of all known three-dimensional protein structures, significantly favored tight turns similar to a type I turn. Of the ten tetrapeptides most closely related to YXRF, eight were surface exposed and had tight-turn conformations, as were four of five tetrapeptides with sequences related to the low density lipoprotein receptor internalization motif, NPXY. The internalization sequences of both receptors contain aromatic residues with intervening hydrogen-bonding residues. Thus, two distinct internalization sequences favor a common structural chemistry and implicate an exposed tight turn as the recognition motif for high efficiency endocytosis.
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“Importantly, the mature human frataxin 81 to 210 was shown to be active enough to rescue frataxin deficiency in cells of FRDA patients (52).”
From Intracellular iron transport and storage: from molecular mechanisms to health implications (2008) · cites this paper as [52]
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Metadata
- Authors
- Collawn, J. F., Stangel, M., Kuhn, L. A., Esekogwu, V., Jing, S., Trowbridge, I. S., & Tainer, J. A.
- Affiliations
- Salk Institute for Biological Studies (US)
- Scripps Clinic (US)
- Scripps Research Institute (US)
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 1990-11
- Volume
- 63
- Issue
- 5
- Pages
- 1061-1072
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W2067691363
- Cited by
- 518
- References
- 68
- Citations by year
- 2026: 4 · 2025: 7 · 2024: 2 · 2023: 3 · 2022: 6 · 2021: 3 · 2020: 4 · 2019: 10 · 2018: 4 · 2017: 2 · 2016: 1 · 2015: 8 · 2014: 3 · 2013: 4 · 2012: 7
- FWCI
- 19.63
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Cell (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Science Foundation
- Arthritis Foundation
- National Institutes of Health (5r01ca034787-11)
- National Cancer Institute (CA 34787)
- National Institute of Diabetes and Digestive and Kidney Diseases (DK07022, T32DK007022)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Receptor Mechanisms and Signaling
- Keywords
- transferrin receptor, endocytosis, NPXY motif, LDL receptor, aromatic residues, hydrogen bonding, cytoplasmic domain, receptor internalization
- MeSH terms
- Amino Acid Sequence, Animals, Cell Membrane, Chick Embryo, Chromosome Deletion, Cytoplasm, Endocytosis, Fibroblasts, Humans, Kinetics, Models, Molecular, Molecular Sequence Data, Protein Conformation, Receptors, LDL, Receptors, Transferrin, Sequence Homology, Nucleic Acid, Transfection, Mutagenesis, Site-Directed
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