Evidence map›Paper›PMID 25673804›Full record

ArticleMolecular biology of the cell2015

Ubiquitin binding by the CUE domain promotes endosomal localization of the Rab5 GEF Vps9.

Tess Shideler, Daniel P Nickerson, Alexey J Merz, Greg Odorizzi

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.6field-weighted citation impact, top 18% 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

16 citing papers in PubMed, 31 citations in OpenAlex.

  1. Endocytosis and trans-Golgi Network in Yeast.Sub-cellular biochemistry · 2026
    Review
  2. Article
  3. ESCRTing the RABs through conversion.Biochemical Society transactions · 2025
    Review
  4. Article
  5. Article
  6. lncRNA HITT inhibits metastasis by attenuating Rab5-mediated endocytosis in lung adenocarcinoma.Molecular therapy : the journal of the American Society of Gene Therapy · 2022
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. PI(3,5)PMolecular biology of the cell · 2018
    Article
  15. Article
  16. 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 3 institutions in 1 country.

Tess ShidelerDepartment of Molecular, Cellular, and Developmental Biology, University of Colorado, Boulder, CO 80309-0347.
Daniel P NickersonDepartment of Biochemistry, University of Washington, Seattle, WA 98195-3750 odorizzi@colorado.edu dpn2@u.washington.edu.
Alexey J MerzDepartment of Biochemistry, University of Washington, Seattle, WA 98195-3750.
Greg OdorizziDepartment of Molecular, Cellular, and Developmental Biology, University of Colorado, Boulder, CO 80309-0347 odorizzi@colorado.edu dpn2@u.washington.edu.
University of Washington · USUniversity of Colorado Boulder · USUniversity of Miami · US

Funding

Dynamics of Endomembrane Docking and FusionR01GM077349 · NIGMS · UNIVERSITY OF WASHINGTON · PI MERZ, ALEXEY JARRELL · 2006 to 2024
$6.1M
Regulation of ESCRT-III Activity in YeastR01GM111335 · NIGMS · UNIVERSITY OF COLORADO · PI ODORIZZI, CHARLES G · 2014 to 2022
$2.6M
NIGMS NIH HHS R01 GM077349NIGMS NIH HHS R01 GM111335NIGMS NIH HHS R01GM-111335
6 · The paper itself

Abstract

Vps9 and Muk1 are guanine nucleotide exchange factors (GEFs) in Saccharomyces cerevisiae that regulate membrane trafficking in the endolysosomal pathway by activating Rab5 GTPases. We show that Vps9 is the primary Rab5 GEF required for biogenesis of late endosomal multivesicular bodies (MVBs). However, only Vps9 (but not Muk1) is required for the formation of aberrant class E compartments that arise upon dysfunction of endosomal sorting complexes required for transport (ESCRTs). ESCRT dysfunction causes ubiquitinated transmembrane proteins to accumulate at endosomes, and we demonstrate that endosomal recruitment of Vps9 is promoted by its ubiquitin-binding CUE domain. Muk1 lacks ubiquitin-binding motifs, but its fusion to the Vps9 CUE domain allows Muk1 to rescue endosome morphology, cargo trafficking, and cellular stress-tolerance phenotypes that result from loss of Vps9 function. These results indicate that ubiquitin binding by the CUE domain promotes Vps9 function in endolysosomal membrane trafficking via promotion of localization.

Indexed as

Amino Acid MotifsEndosomal Sorting Complexes Required for TransportGuanine Nucleotide Exchange FactorsMultivesicular BodiesProtein BindingProtein Interaction Domains and MotifsProtein TransportSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsUbiquitinsVesicular Transport ProteinsEndosomal Sorting Complexes Required for TransportGuanine Nucleotide Exchange FactorsMuk1 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsUbiquitinsVesicular Transport ProteinsVPS9 protein, S cerevisiae

Identifiers

PMID25673804
PMCPMC4454180
OpenAlexW2316921686

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.