Evidence map›Paper›PMID 22284051›Full record

ArticleTraffic (Copenhagen, Denmark)2012

Rabankyrin-5 interacts with EHD1 and Vps26 to regulate endocytic trafficking and retromer function.

Jing Zhang, Calliste Reiling, James B Reinecke, Iztok Prislan, Luis A Marky, Paul L Sorgen, Naava Naslavsky, Steve Caplan

Abstract read
In one paragraph

Article in Traffic (Copenhagen, Denmark), 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
–field-weighted citation impact
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

41 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. The Rab5 effector Rabankyrin-5 mediates endosomal fusion and trafficking of human papillomavirus during early entry.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  5. The endocytic fission protein EHD1 interacts with tubulin and regulates microtubule function.Biochimica et biophysica acta. Molecular cell research · 2026
    Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Receptor Recycling by Retromer.Molecular and cellular biology · 2023
    Review
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
  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

8 authors.

Jing ZhangDepartment of Biochemistry and Molecular Biology and Eppley Cancer Center, University of Nebraska Medical Center, Omaha, NE 68198-5870, USA.
Calliste Reiling
James B Reinecke
Iztok Prislan
Luis A Marky
Paul L Sorgen
Naava Naslavsky
Steve Caplan

Funding

SUPPRESSIVE ROLE OF TGFBETA IN METASTASIS OF COLON CANCERP20RR018759 · NCRR · UNIVERSITY OF NEBRASKA MEDICAL CENTER · PI JOHNSON, KEITH R · 2003 to 2011
$17.9M
Molecular Mechanisms Controlling Endocytic RecyclingR01GM074876 · NIGMS · UNIVERSITY OF NEBRASKA MEDICAL CENTER · PI CAPLAN, STEVEN H · 2006 to 2015
$2.6M
Regulation of EHD protein function by molecular partner interactionsR01GM087455 · NIGMS · UNIVERSITY OF NEBRASKA MEDICAL CENTER · PI CAPLAN, STEVEN H, SORGEN, PAUL L · 2010 to 2013
$1.1M
ITC Ultrasensitive Microcalorimeter for Measuring Biomolecular InteractionsS10RR027205 · NCRR · UNIVERSITY OF NEBRASKA MEDICAL CENTER · PI MARKY, LUIS ARNALDO · 2010 to 2010
$125k
NCRR NIH HHS 1S10RR027205NCRR NIH HHS P20 RR018759NCRR NIH HHS S10 RR027205NIGMS NIH HHS R01 GM074876NIGMS NIH HHS R01GM074876NIGMS NIH HHS R01 GM087455NIGMS NIH HHS R01GM087455
6 · The paper itself

Abstract

Rabankyrin-5 (Rank-5) has been implicated as an effector of the small GTPase Rab5 and plays an important role in macropinocytosis. We have now identified Rank-5 as an interaction partner for the recycling regulatory protein, Eps15 homology domain 1 (EHD1). We have demonstrated this interaction by glutathione S-transferase-pulldown, yeast two-hybrid assay, isothermal calorimetry and co-immunoprecipitation, and found that the binding occurs between the EH domain of EHD1 and the NPFED motif of Rank-5. Similar to EHD1, we found that Rank-5 colocalizes and interacts with components of the retromer complex such as vacuolar protein sorting 26 (Vps26), suggesting a role for Rank-5 in retromer-based transport. Indeed, depletion of Rank-5 causes mislocalization of Vps26 and affects both the retrieval of mannose 6-phosphate receptor transport to the Golgi from endosomes and biosynthetic transport. Moreover, Rank-5 is required for normal retromer distribution, as overexpression of a wild-type Rank-5-small interfering RNA-resistant construct rescues retromer mislocalization. Finally, we show that depletion of either Rank-5 or EHD1 impairs secretion of vesicular stomatitis virus glycoprotein. Overall, our data identify a new interaction between Rank-5 and EHD1, and novel endocytic regulatory roles that include retromer-based transport and secretion.

Indexed as

EndocytosisAmino Acid MotifsAnimalsBiological TransportCathepsin GEndosomesGreen Fluorescent ProteinsHeLa CellsHumansMembrane GlycoproteinsMembrane ProteinsModels, BiologicalPhosphate-Binding Proteinsrab5 GTP-Binding ProteinsThermodynamicsTwo-Hybrid System TechniquesANKFY1 protein, humanCathepsin GEHD1 protein, humanG protein, vesicular stomatitis virusGreen Fluorescent ProteinsMembrane GlycoproteinsMembrane ProteinsPhosphate-Binding Proteinsrab5 GTP-Binding ProteinsVesicular Transport ProteinsViral Envelope ProteinsVPS26A protein, human

Identifiers

PMID22284051
PMCPMC3613124

What OpenQuestion holds

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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.