Evidence map›Paper›PMID 25059659›Full record

ArticleThe Journal of biological chemistry2014

Structural determinants for binding of sorting nexin 17 (SNX17) to the cytoplasmic adaptor protein Krev interaction trapped 1 (KRIT1).

Amy L Stiegler, Rong Zhang, Weizhi Liu, Titus J Boggon

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
1.1field-weighted citation impact, top 26% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

24 citing papers in PubMed, 33 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Endo-IP and lyso-IP toolkit for endolysosomal profiling of human-induced neurons.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  5. Article
  6. Article
  7. KRIT1 in vascular biology and beyond.Bioscience reports · 2024
    Review
  8. Structural basis for Retriever-SNX17 assembly and endosomal sorting.bioRxiv : the preprint server for biology · 2024
    Article
  9. Article
  10. Review
  11. Review
  12. Review
  13. Article
  14. Crystal structure of the FERM-folded talin head reveals the determinants for integrin binding.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Myosin MyTH4-FERM structures highlight important principles of convergent evolution.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 1 institution in 1 country.

Amy L StieglerFrom the Department of Pharmacology, Yale University School of Medicine, New Haven, Connecticut 06520 amy.stiegler@yale.edu.
Rong ZhangFrom the Department of Pharmacology, Yale University School of Medicine, New Haven, Connecticut 06520.
Weizhi LiuFrom the Department of Pharmacology, Yale University School of Medicine, New Haven, Connecticut 06520.
Titus J BoggonFrom the Department of Pharmacology, Yale University School of Medicine, New Haven, Connecticut 06520 titus.boggon@yale.edu.
Yale University · US

Funding

Molecular assembly and regulation of the cerebral cavernous malformation complexR01NS085078 · NINDS · YALE UNIVERSITY · PI BOGGON, TITUS JONATHON, CALDERWOOD, DAVID A · 2013 to 2017
$1.8M
NINDS NIH HHS R01 NS085078
6 · The paper itself

Abstract

Sorting nexin 17 (SNX17) is a member of the family of cytoplasmic sorting nexin adaptor proteins that regulate endosomal trafficking of cell surface proteins. SNX17 localizes to early endosomes where it directly binds NPX(Y/F) motifs in the cytoplasmic tails of its target receptors to mediate their rates of endocytic internalization, recycling, and/or degradation. SNX17 has also been implicated in mediating cell signaling and can interact with cytoplasmic proteins. KRIT1 (Krev interaction trapped 1), a cytoplasmic adaptor protein associated with cerebral cavernous malformations, has previously been shown to interact with SNX17. Here, we demonstrate that SNX17 indeed binds directly to KRIT1 and map the binding to the second Asn-Pro-Xaa-Tyr/Phe (NPX(Y/F)) motif in KRIT1. We further characterize the interaction as being mediated by the FERM domain of SNX17. We present the co-crystal structure of SNX17-FERM with the KRIT1-NPXF2 peptide to 3.0 Å resolution and demonstrate that the interaction is highly similar in structure and binding affinity to that between SNX17 and P-selectin. We verify the molecular details of the interaction by site-directed mutagenesis and pulldown assay and thereby confirm that the major binding site for SNX17 is confined to the NPXF2 motif in KRIT1. Taken together, our results verify a direct interaction between SNX17 and KRIT1 and classify KRIT1 as a SNX17 binding partner.

Indexed as

Amino Acid MotifsAmino Acid SequenceBinding, CompetitiveBinding SitesCrystallography, X-RayHumansImmunoblottingKRIT1 ProteinMicrotubule-Associated ProteinsModels, MolecularMutagenesis, Site-DirectedProtein BindingProtein Interaction MappingProtein Structure, TertiaryProto-Oncogene ProteinsP-SelectinKRIT1 ProteinKRIT1 protein, humanMicrotubule-Associated ProteinsProto-Oncogene ProteinsP-SelectinSNX17 protein, humanSorting NexinsCerebral Cavernous MalformationsCrystal StructureFERM DomainKRIT1NPXY MotifPeptide InteractionProtein DomainProtein MotifProtein-Protein InteractionSorting Nexin

Identifiers

PMID25059659
PMCPMC4155697
OpenAlexW2060568604

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.