Cited by 39Cellular transport and secretionProtein Kinase Regulation and GTPase SignalingCaveolin-1 and cellular processes

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Sorting nexin 17, a non-self-assembling and a PtdIns(3)P high class affinity protein, interacts with the cerebral cavernous malformation related protein KRIT1

Czubayko, Martin, Knauth, Peter, Schlüter, Thomas, Florian, Volker, Bohnensack, Ralf·2006·Biochemical and Biophysical Research Communications

Abstract

The mammalian sorting nexin (SNX) proteins are involved in the endocytosis and the sorting machinery of transmembrane proteins. Additionally to the family defining phox homology (PX) domain, SNX17 is the only member with a truncated FERM (4.1, ezrin, radixin, and moesin) domain and a unique C-terminal region (together designated as FC unit). By gel filtration and lipid overlay assays we show that SNX17 is a non-self-assembling and a PtdIns(3)P high class affinity protein. A SNX17 affinity to any other phosphoinositides was not detected. By yeast two-hybrid- and GST-trapping assays we identified KRIT1 (krev1 interaction trapped 1) as a new specific interaction partner of the FC unit of SNX17. KRIT1 binds SNX17 by its N-terminal region like the known interaction partner ICAP1alpha (integrin cytoplasmic domain-associated protein-1). The interaction was also detected in HEK 293 cells transiently expressing GFP-tagged KRIT1 and Xpress-tagged SNX17. KRIT1 mutations cause cerebral cavernous malformation (CCM1). Our finding suggests a SNX17 involvement in the indicated KRIT1 function in cell adhesion processes by integrin signaling.

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Crossref · 10.1016/j.bbrc.2006.04.129

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  • The SNX17 PX domain facilitates interaction between SNX17 and PI3P-enriched membranes, particularly early endosome membranes that are positive for EEA1.

    “Its PX domain facilitates the interaction between SNX17 and PI3P-enriched membranes, particularly with the early endosome membranes that are positive for EEA1 [27]–[29].”

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Metadata

Authors
Czubayko, M., Knauth, P., Schlüter, T., Florian, V., & Bohnensack, R.
Affiliations
  • Otto-von-Guericke-Universität Magdeburg (DE)
  • Universidad de Guadalajara (MX)
Corresponding author
Bohnensack, Ralf
Venue
Biochemical and Biophysical Research Communications
Publisher
Elsevier BV
Published
2006-07
Volume
345
Issue
3
Pages
1264-1272
ISSN
0006-291X (ISSN-L)
OpenAlex
W2000183806
Cited by
39
References
4
Citations by year
2023: 1 · 2022: 2 · 2021: 4 · 2020: 3 · 2019: 1 · 2018: 1 · 2017: 1 · 2015: 1 · 2014: 3 · 2013: 3 · 2012: 1
FWCI
1.16
Type
journal article
Language
en
Open access
closed
Locations
  • Biochemical and Biophysical Research Communications (publishedVersion)
  • PubMed (publishedVersion)
Funders
  • U.S. Department of Health and Human Services
  • National University of Singapore
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Caveolin-1 and cellular processes
Keywords
SNX17, KRIT1, cerebral cavernous malformations, PtdIns(3)P, FERM domain, protein-protein interaction, phosphoinositide binding, integrin signaling, cell adhesion, endocytosis
MeSH terms
KRIT1 Protein, Carrier Proteins, Cell Communication, Chromatography, Gel, Glutathione, Humans, Kinetics, Microtubule-Associated Proteins, Phosphatidylinositols, Proto-Oncogene Proteins, Integrins, Protein Structure, Tertiary, Phosphatidylinositol 3-Kinases, Hemangioma, Cavernous, Central Nervous System, Two-Hybrid System Techniques, Vesicular Transport Proteins, Endothelial Cells, Sorting Nexins

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