The DOI matches its Crossref record; 42 of the 42 references it cites were found in a registry or an index.
Identification of a Family of Sorting Nexin Molecules and Characterization of Their Association with Receptors
Open accessAbstract
Sorting nexin 1 (SNX1) is a protein that binds to the epidermal growth factor (EGF) receptor and is proposed to play a role in directing EGF receptors to lysosomes for degradation (R. C. Kurten, D. L. Cadena, and G. N. Gill, Science 272:1008-1010, 1996). We have obtained full-length cDNAs and deduced the amino acid sequences of three novel homologous proteins, which were denoted human sorting nexins (SNX2, SNX3, and SNX4). In addition, we identified a presumed splice variant isoform of SNX1 (SNX1A). These molecules contain a conserved domain of approximately 100 amino acids, which was termed the phox homology (PX) domain. Human SNX1 (522 amino acids), SNX1A (457 amino acids), SNX2 (519 amino acids), SNX3 (162 amino acids), and SNX4 (450 amino acids) are part of a larger family of hydrophilic molecules including proteins identified in Caenorhabditis elegans and Saccharomyces cerevisiae. Despite their hydrophilic nature, the sorting nexins are found partially associated with cellular membranes. They are widely expressed, although the tissue distribution of each sorting nexin mRNA varies. When expressed in COS7 cells, epitope-tagged sorting nexins SNX1, SNX1A, SNX2, and SNX4 coimmunoprecipitated with receptor tyrosine kinases for EGF, platelet-derived growth factor, and insulin. These sorting nexins also associated with the long isoform of the leptin receptor but not with the short and medium isoforms. Interestingly, endogenous COS7 transferrin receptors associated exclusively with SNX1 and SNX1A, while SNX3 was not found to associate with any of the receptors studied. Our demonstration of a large conserved family of sorting nexins that interact with a variety of receptor types suggests that these proteins may be involved in several stages of intracellular trafficking in mammalian cells.
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“The influence of SNXs on a lipid level may be because of the interaction of SNX1, SNX2, and SNX4 with leptin receptors [132].”
From Insights of Endocytosis Signaling in Health and Disease (2023) · cites this paper as [132]
In the citing paper
“Several members of the sorting nexin family have been shown to interact with transmembrane receptors involved in cell signaling (8), in some cases via their carboxyl-terminal domain (23) and in others, via the PX domain (28).”
From Sorting Motifs in the Intracellular Domain of the Low Density Lipoprotein Receptor Interact with a Novel Domain of Sorting Nexin-17 (2004) · cites this paper as [8]
In the citing paper
“These authors assigned the protein to the sorting nexin family as sorting nexin-17 (SNX17), based on the presence of a characteristic PX domain (8).”
From Sorting Motifs in the Intracellular Domain of the Low Density Lipoprotein Receptor Interact with a Novel Domain of Sorting Nexin-17 (2004) · cites this paper as [8]
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Metadata
- Authors
- Haft, C. R., de la Luz Sierra, M., Barr, V. A., Haft, D. H., & Taylor, S. I.
- Affiliations
- National Institutes of Health (US)
- 1Diabetes Branch, National Institutes of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892
- Biomedical Research Foundation (US)
- Corresponding author
- Haft, Carol Renfrew
- Venue
- Molecular and Cellular Biology
- Publisher
- Informa UK Limited
- Published
- 1998-12-01
- Volume
- 18
- Issue
- 12
- Pages
- 7278-7287
- ISSN
- 0270-7306 (ISSN-L)
- 1098-5549
- PMC
- PMC109309
- OpenAlex
- W2107502575
- Cited by
- 244
- References
- 42
- Citations by year
- 2026: 1 · 2025: 4 · 2024: 4 · 2023: 5 · 2022: 7 · 2021: 6 · 2020: 10 · 2019: 5 · 2018: 5 · 2017: 7 · 2016: 4 · 2015: 3 · 2014: 5 · 2013: 4 · 2012: 11
- FWCI
- 4.58
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Molecular and Cellular Biology (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Receptor Mechanisms and Signaling
- Keywords
- sorting nexins, SNX1, SNX2, SNX3, SNX4, phox homology domain, EGF receptor, receptor tyrosine kinase, leptin receptor isoforms, transferrin receptor, receptor degradation, lysosomal degradation, intracellular trafficking, splice variants, membrane association, protein-protein interaction
- MeSH terms
- Amino Acid Sequence, Animals, Carrier Proteins, Cell Membrane, Cells, Cultured, Cloning, Molecular, Fungal Proteins, Humans, Molecular Sequence Data, Protein Binding, Receptors, Cell Surface, RNA, Messenger, Helminth Proteins, Sequence Homology, Amino Acid, Alternative Splicing, Sequence Analysis, DNA, Vesicular Transport Proteins, ErbB Receptors
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