Sorting Nexin 17 Accelerates Internalization Yet Retards Degradation of P-selectin
Open accessAbstract
The transient appearance of P-selectin on the surface of endothelial cells helps recruit leukocytes into sites of inflammation. The tight control of cell surface P-selectin on these cells depends on regulated exocytosis of Weibel-Palade bodies where the protein is stored and on its rapid endocytosis. After endocytosis, P-selectin is either sorted via endosomes and the Golgi apparatus for storage in Weibel-Palade bodies or targeted to lysosomes for degradation. A potential player in this complex endocytic itinerary is SNX17, a member of the sorting nexin family, which has been shown in a yeast two-hybrid assay to bind P-selectin. Here, we show that overexpression of SNX17 in mammalian cells can influence two key steps in the endocytic trafficking of P-selectin. First, it promotes the endocytosis of P-selectin from the plasma membrane. Second, it inhibits the movement of P-selectin into lysosomes, thereby reducing its degradation.
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SNX17 is an adaptor protein localized in the early endosome compartment, mostly due to interaction of its PX domain with early endosomal PI(3)P phospholipids.
“SNX17 is an adaptor protein that is localized in the early endosome compartment [28], [30], [31], mostly due to the interaction of its PX domain with the characteristic early endosomal PI(3)P phospholipids [31], [60].”
From Sorting nexin 17 regulates ApoER2 recycling and reelin signaling (2014) · cites this paper as [30]
The Introduction places SNX17 in an early endosomal compartment, and “Targeting of SNX17” reports that its PX domain and PI-3-kinase activity are needed for endosomal localization. That section identifies PI(3)P binding as the most likely mechanism, but does not establish that localization is mostly due to that interaction; it also suggests additional protein interactions may determine SNX17’s location within endosomes. (LLM, conf=0.82)
Experimental — accuracy not yet measuredSNX17 increases the endocytosis of P-selectin and diminishes the transport of this membrane protein to the late endosome.
“SNX17 increases the endocytosis of P-selectin and diminishes the transport of this membrane protein to the late endosome [30].”
From Sorting nexin 17 regulates ApoER2 recycling and reelin signaling (2014) · cites this paper as [30]
Overexpression of SNX17 increases P-selectin recycling while avoiding entry into multivesicular bodies/late endosomes.
“In the case of P-selectin, the overexpression of SNX17 concomitant with the increase in the receptor endocytosis, increases its recycling [30] while avoiding entry into the multivesicular bodies/late endosomes [60].”
From Sorting nexin 17 regulates ApoER2 recycling and reelin signaling (2014) · cites this paper as [30]
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Research works printed but not linked: 1
- Zhong, Q. Lazar, C.S., Tronche `re, H., Sato, T.K., Meerloo, T., Yeo, M., Songyang, Z., Emr, S.D., and Gill, G.N. (2002). Endosomal localization and function of sorting nexin 1. Proc. Natl. Acad. Sci. USA 99 , 6767-6772.
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To degrade or not to degrade: Mechanisms and significance of endocytic recycling
Cullen, P. J., & Steinberg, F. (2018) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-018-0053-7 · Cited by 590 · see citing works
Sorting nexin 17 regulates ApoER2 recycling and reelin signaling
Sotelo, P., Farfán, P., Benitez, M. L., Bu, G., & Marzolo, M.-P. (2014) · PLoS ONE · doi:10.1371/journal.pone.0093672 · Cited by 47 · see citing works
- Authors
- Williams, R., Schlüter, T., Roberts, M. S., Knauth, P., Bohnensack, R., & Cutler, D. F.
- Affiliations
- MRC Laboratory for Molecular Cell Biology (GB)
- Otto-von-Guericke-Universität Magdeburg (DE)
- Venue
- Molecular Biology of the Cell
- Published
- 2004-07
- Volume
- 15
- Issue
- 7
- Pages
- 3095-3105
- ISSN
- 1059-1524 (ISSN-L)
- 1939-4586
- PMC
- PMC452567
- OpenAlex
- W2164979127
- Cited by
- 44
- References
- 0
- Citations by year
- 2025: 1 · 2024: 2 · 2023: 1 · 2022: 2 · 2021: 3 · 2020: 1 · 2019: 2 · 2018: 2 · 2015: 3 · 2014: 2 · 2013: 3 · 2012: 3
- FWCI
- 1.27
- Type
- journal article
- Language
- en
- Open access
- green
- europepmc.org
- Locations
- Molecular Biology of the Cell (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- UCL Discovery (University College London) (submittedVersion)
- Funders
- Medical Research Council
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Health Sciences › Medicine › Immunology and Allergy › Cell Adhesion Molecules Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Extracellular vesicles in disease
- Keywords
- P-selectin, SNX17, sorting nexins, endocytosis, lysosomal degradation, Weibel-Palade bodies, exocytosis, endosomal trafficking, Golgi apparatus, endothelial cells, leukocyte recruitment, inflammation
- MeSH terms
- Wortmannin, Phosphoinositide-3 Kinase Inhibitors, Androstadienes, Animals, Carrier Proteins, Cell Membrane, Cells, Cultured, Endocytosis, Humans, Lysosomes, Endosomes, Gene Expression, Protein Structure, Tertiary, P-Selectin, Phosphatidylinositol 3-Kinases, Protein Transport, Vesicular Transport Proteins, Sorting Nexins
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