Evidence map›Paper›PMID 32041776›Full record

ArticleThe Journal of biological chemistry2020

Sorting nexin 17 (SNX17) links endosomal sorting to Eps15 homology domain protein 1 (EHD1)-mediated fission machinery.

Kanika Dhawan, Naava Naslavsky, Steve Caplan

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
2.1field-weighted citation impact, top 14% 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

23 citing papers in PubMed, 33 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. The endocytic fission protein EHD1 interacts with tubulin and regulates microtubule function.Biochimica et biophysica acta. Molecular cell research · 2026
    Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. A missense mutation inFrontiers in cell and developmental biology · 2023
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Review
  20. Review
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

3 authors at 2 institutions in 1 country.

Kanika DhawanDepartment of Biochemistry and Molecular Biology University of Nebraska Medical Center, Omaha, Nebraska 68198.
Naava NaslavskyDepartment of Biochemistry and Molecular Biology University of Nebraska Medical Center, Omaha, Nebraska 68198.
Steve CaplanDepartment of Biochemistry and Molecular Biology University of Nebraska Medical Center, Omaha, Nebraska 68198 scaplan@unmc.edu.ORCID 0000-0001-9445-4297
University of Nebraska Medical Center · USNebraska Medical Center · US

Funding

UNMC Structural Biology CoreP20GM103427 · NIGMS · UNIVERSITY OF NEBRASKA MEDICAL CENTER · PI PAUL L SORGEN · 2012 to 2026
$59.2M
UNMC/EPPLEY CANCER CENTER SUPPORT GRANTP30CA036727 · NCI · UNIVERSITY OF NEBRASKA MEDICAL CENTER · PI Joann B. Sweasy · 1985 to 2026
$55.0M
Research Pilot Project ProgramP30GM106397 · NIGMS · UNIVERSITY OF NEBRASKA MEDICAL CENTER · PI JOHNSON, KEITH R · 2013 to 2017
$4.9M
Mechanisms and function of endosome-derived tubular carriersR01GM123557 · NIGMS · UNIVERSITY OF NEBRASKA MEDICAL CENTER · PI CAPLAN, STEVEN H · 2017 to 2020
$1.3M
NCI NIH HHS P30 CA036727NIGMS NIH HHS P20 GM103427NIGMS NIH HHS P30 GM106397NIGMS NIH HHS R01 GM123557
6 · The paper itself

Abstract

Following endocytosis, receptors that are internalized to sorting endosomes are sorted to different pathways, in part by sorting nexin (SNX) proteins. Notably, SNX17 interacts with a multitude of receptors in a sequence-specific manner to regulate their recycling. However, the mechanisms by which SNX17-labeled vesicles that contain sorted receptors bud and undergo vesicular fission from the sorting endosomes remain elusive. Recent studies suggest that a dynamin-homolog, Eps15 homology domain protein 1, catalyzes fission and releases endosome-derived vesicles for recycling to the plasma membrane. However, the mechanism by which EHD1 is coupled to various receptors and regulates their recycling remains unknown. Here we sought to characterize the mechanism by which EHD1 couples with SNX17 to regulate recycling of SNX17-interacting receptors. We hypothesized that SNX17 couples receptors to the EHD1 fission machinery in mammalian cells. Coimmunoprecipitation experiments and

Indexed as

AnimalsCell MembraneEndosomesGene EditingHeLa CellsHumansLow Density Lipoprotein Receptor-Related Protein-1MiceMutagenesis, Site-DirectedNIH 3T3 CellsProtein BindingRecombinant ProteinsRNA InterferenceRNA, Small InterferingSorting NexinsVesicular Transport ProteinsEhd1 protein, mouseLow Density Lipoprotein Receptor-Related Protein-1Recombinant ProteinsRNA, Small InterferingSnx17 protein, mouseSorting NexinsVesicular Transport Proteinsendocytosisendosomal fissionendosomeEps15 homology domain protein 1 (EHD1)intracellular traffickingLDL receptor–related protein 1 (LRP1)receptorreceptor endocytosisreceptor recyclingretromersortingsorting nexin 17 (SNX17)sorting nexin (SNX)traffickingvesicles

Identifiers

PMID32041776
PMCPMC7086038
OpenAlexW3006483309

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.