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

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

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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  1. Cauchy, 1847, Méthode générale pour la résolution des systèmes d'équations simultanées, C. R. Hebd. Seances Acad. Sci., 25, 536

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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)
ORCID
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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