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Cited by 55Cellular transport and secretionAutophagy in Disease and TherapyCalcium signaling and nucleotide metabolism

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Functions of Sorting Nexin 17 Domains and Recognition Motif for P-selectin Trafficking

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Knauth, Peter, Schlüter, Thomas, Czubayko, Martin, Kirsch, Cornelia, Florian, Volker, Schreckenberger, Susan, Hahn, Heidi, Bohnensack, Ralf·2005·Journal of Molecular Biology
DOI 10.1016/j.jmb.2005.02.004
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Abstract

SNX17 is a member of the sorting nexin family (SNX), a group of hydrophilic proteins whose common characteristic property is a phox homology (PX) domain. The PX domain directs SNXs to phosphatidylinositides containing membranes of the endosomal compartment, where the SNXs are involved in the sorting of transmembrane proteins. SNX17 is known to interact with P-selectin and the LDL receptor family. Here, we report that the PX domain of SNX17 specifically binds to phosphatidylinositol 3-phosphate-containing membranes. The functional part of SNX17 that binds P-selectin or Patched (PTCH) consists of a truncated FERM domain and a unique C terminus together (FC-unit). In a yeast two-hybrid analysis a putative recognition motif for the FC-unit was revealed within P-selectin as FxNaa(F/Y). When HepG2 cells overexpress P-selectin together with SNX17, SNX17 changes its distribution from early endosomes to lysobisphosphatidic acid-containing late endosomes. Furthermore, overexpressed SNX17 restrains P-selectin in the outer membrane of the late endosomal compartment, thus preventing the normal lysosomal accumulation of P-selectin. These results suggest that the PX domain is necessary for the intracellular localisation, while the FC-unit is required for cargo recognition. We hypothesise that the expression level of SNX17 may regulate the lysosomal degradation, at least for P-selectin, by suppressing its entry into the inner vesicles of the multi-vesicular bodies (MVBs).

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  • A similar region (FERM domain plus C-terminal region) was proposed for the interaction of SNX17 with P-selectin.

    “A similar region (FERM domain plus C-terminal region) was also proposed for the interaction of SNX17 with P-selectin, a protein that is not a member of the LDL-R superfamily [60].”

    From Sorting nexin 17 regulates ApoER2 recycling and reelin signaling (2014) · cites this paper as [60]

  • 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 [60]

  • Both SNX17 and SNX27 can interact with PI(3)P through their PX domains.

    “both interact with the signaling lipid PI(3)P via their PX domains”

    From PI(3)P coordinates SNX17- and SNX27-dependent protein recycling for long-term synaptic plasticity (2025) · cites this paper as Knauth et al., 2005

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Metadata

Authors
Knauth, P., Schlüter, T., Czubayko, M., Kirsch, C., Florian, V., Schreckenberger, S., Hahn, H., & Bohnensack, R.
Affiliations
  • Centro de Investigación y Asistencia en Tecnología y Diseño del Estado de Jalisco (MX)
  • Otto-von-Guericke-Universität Magdeburg (DE)
  • Friedrich Schiller University Jena (DE)
  • University of Göttingen (DE)
Corresponding author
Knauth, Peter
ORCID
Venue
Journal of Molecular Biology
Publisher
Elsevier BV
Published
2005-04
Volume
347
Issue
4
Pages
813-825
ISSN
0022-2836 (ISSN-L)
DOI
10.1016/j.jmb.2005.02.004
OpenAlex
W2083727544
Cited by
55
References
4
Citations by year
2025: 3 · 2024: 1 · 2023: 1 · 2022: 1 · 2021: 9 · 2020: 4 · 2018: 2 · 2015: 4 · 2014: 5 · 2013: 4 · 2012: 4
FWCI
1.22
Type
journal article
Language
en
Open access
Licence
Locations
  • Journal of Molecular Biology (publishedVersion)
  • PubMed (publishedVersion)
  • GRO (submittedVersion, cc-by)
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 › Physiology › Calcium signaling and nucleotide metabolism
Keywords
SNX17, sorting nexins, P-selectin, PX domain, phosphatidylinositol 3-phosphate, FERM domain, late endosomes, lysosomal degradation, multivesicular bodies, endosomal sorting, LDL receptor family, Patched
MeSH terms
Amino Acid Sequence, Animals, Carrier Proteins, Cell Line, Cricetinae, Humans, Molecular Sequence Data, Mutation, Protein Binding, Endosomes, Substrate Specificity, Gene Expression, Protein Structure, Tertiary, Phosphatidylinositol Phosphates, P-Selectin, Amino Acid Motifs, Protein Transport, Vesicular Transport Proteins

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