Cited by 518Cellular transport and secretionProtein Structure and DynamicsReceptor Mechanisms and Signaling

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Transferrin receptor internalization sequence YXRF implicates a tight turn as the structural recognition motif for endocytosis

Collawn, James F., Stangel, Martin, Kuhn, Leslie A., Esekogwu, Victor, Jing, Shuqian, Trowbridge, Ian S., Tainer, John A.·1990·Cell

DOI 10.1016/0092-8674(90)90509-d

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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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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)
ORCID: Collawn, James F.
Stangel, Martin
Kuhn, Leslie A.
Tainer, John A.
Venue: Cell
Publisher: Elsevier BV
Published: 1990-11
Volume: 63
Issue: 5
Pages: 1061-1072
ISSN: 0092-8674 (ISSN-L)
DOI: 10.1016/0092-8674(90)90509-d
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
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
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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Transferrin receptor internalization sequence YXRF implicates a tight turn as the structural recognition motif for endocytosis

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