Cited by 244Cellular transport and secretionAutophagy in Disease and TherapyReceptor Mechanisms and Signaling

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Identification of a Family of Sorting Nexin Molecules and Characterization of Their Association with Receptors

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Haft, Carol Renfrew, de la Luz Sierra, Maria, Barr, Valarie A., Haft, Daniel H., Taylor, Simeon I.·1998·Molecular and Cellular Biology

DOI 10.1128/mcb.18.12.7278PMC PMC109309

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Abstract

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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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
ORCID: Haft, Carol Renfrew
Barr, Valarie A.
Haft, Daniel H.
Taylor, Simeon I.
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
DOI: 10.1128/mcb.18.12.7278
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
Licence: journals.asm.org/non-commercial-tdm-license (tdm)
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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Identification of a Family of Sorting Nexin Molecules and Characterization of Their Association with Receptors

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