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Cited by 26Cellular transport and secretionCholesterol and Lipid MetabolismPhagocytosis and Immune Regulation

The DOI matches its Crossref record; 4 of the 4 references it cites were found in a registry or an index.

Adaptor protein sorting nexin 17 interacts with the scavenger receptor FEEL-1/stabilin-1 and modulates its expression on the cell surface

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Adachi, Hideki, Tsujimoto, Masafumi·2010·Biochimica et Biophysica Acta (BBA) - Molecular Cell Research
DOI 10.1016/j.bbamcr.2010.02.011
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Abstract

The scavenger receptor FEEL-1/stabilin-1 is known as the marker of alternatively activated macrophage and sinusoidal endothelial cell. FEEL-1/stabilin-1 is a multifunctional transmembrane glycoprotein that is implicated in bacterial infection, diabetes, atherosclerosis, wound healing, and innate immunity. In the current study, we have identified the phox-homology domain containing protein SNX17 as a novel interaction partner of FEEL-1/stabilin-1 in endothelial cells. SNX17 directly interacts with FEEL-1/stabilin-1 and regulates its trafficking. Studies using the cytoplasmic domain of truncated or mutant FEEL-1/stabilin-1 suggest that the NPxF motif of the FEEL-1/stabilin-1 cytoplasmic tail is required for its interaction with SNX17. By transfecting cells with small interfering RNA targeting SNX17, total cellular FEEL-1/stabilin-1 expression and FEEL-1/stabilin-1-mediated ligand uptake were significantly decreased due to the enhancement of FEEL-1/stabilin-1 protein degradation. Our results identify SNX17 as a novel interaction partner of FEEL-1/stabilin-1 in endothelial cells.

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  • SNX17 interacts with its partner when the tyrosine is replaced with a phenylalanine, as is the case for Stabilin1.

    “SNX17 also interacts with its partner when the tyrosine is replaced with a phenylalanine [59], as is the case for Stabilin1.”

    From Sorting nexin 17 regulates ApoER2 recycling and reelin signaling (2014) · cites this paper as [59]

  • The region 150-470 of SNX17 is the interacting domain for LRP1 and the scavenger receptor Stabilin1.

    “Similarly, it has been shown for LRP1 and the scavenger receptor Stabilin1, that the region of 150–470 of SNX17 is the interacting domain [31], [59].”

    From Sorting nexin 17 regulates ApoER2 recycling and reelin signaling (2014) · cites this paper as [59]

Citations

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Research works printed but not linked: 26

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Metadata

Authors
Adachi, H., & Tsujimoto, M.
Affiliations
RIKEN (JP)
Corresponding author
Adachi, Hideki
Venue
Biochimica et Biophysica Acta (BBA) - Molecular Cell Research
Publisher
Elsevier BV
Published
2010-05
Volume
1803
Issue
5
Pages
553-563
ISSN
0167-4889 (ISSN-L)
DOI
10.1016/j.bbamcr.2010.02.011
OpenAlex
W2022508704
Cited by
26
References
4
Citations by year
2025: 1 · 2024: 1 · 2020: 1 · 2018: 1 · 2017: 3 · 2015: 3 · 2014: 3 · 2013: 3 · 2012: 3
FWCI
1.82
Type
journal article
Language
en
Open access
Licence
Locations
  • Biochimica et Biophysica Acta (BBA) - Molecular Cell Research (publishedVersion)
  • PubMed (publishedVersion)
Funders
  • Ministry of Education, Culture, Sports, Science, and Technology
  • MEXT
  • RIKEN
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Cholesterol and Lipid Metabolism
  • Life Sciences › Immunology and Microbiology › Immunology › Phagocytosis and Immune Regulation
Keywords
SNX17, scavenger receptors, protein-protein interaction, protein trafficking, protein degradation, ligand uptake, endothelial cells, M2 macrophages, sinusoidal endothelial cells, phox homology domain
MeSH terms
Amino Acid Sequence, Cell Membrane, Cells, Cultured, Endothelium, Vascular, Humans, Molecular Sequence Data, Umbilical Veins, Gene Library, Cell Adhesion Molecules, Neuronal, Receptors, Lymphocyte Homing, Sequence Homology, Amino Acid, Protein Structure, Tertiary, Two-Hybrid System Techniques, Vesicular Transport Proteins, RNA, Small Interfering, Sorting Nexins

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