Evidence map›Paper›PMID 17699593›Full record

ArticleMolecular biology of the cell2007

Rabaptin-5-independent membrane targeting and Rab5 activation by Rabex-5 in the cell.

Huaiping Zhu, Guangyu Zhu, Jay Liu, Zhimin Liang, Xuejun C Zhang, Guangpu Li

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing 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

34 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. RABEP1 amplifies front signaling in neutrophil migration.bioRxiv : the preprint server for biology · 2025
    Article
  5. ESCRTing the RABs through conversion.Biochemical Society transactions · 2025
    Review
  6. Rab21 recruits EEA1 and competes with Rab5 for Rabex-5 activation.Frontiers in cell and developmental biology · 2025
    Article
  7. Article
  8. Review
  9. Article
  10. Stochastic activation and bistability in a Rab GTPase regulatory network.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  11. Article
  12. Article
  13. Article
  14. Elevated RABEX-5 protein expression predicts poor prognosis in combined small cell lung cancer.Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2015
    Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. 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

6 authors.

Huaiping ZhuDepartment of Biochemistry and Molecular Biology, University of Oklahoma Health Sciences Center, Oklahoma City, OK 73104, USA.
Guangyu Zhu
Jay Liu
Zhimin Liang
Xuejun C Zhang
Guangpu Li

Funding

Structural and Functional Specificity of Rab GTPasesR01GM074692 · NIGMS · UNIVERSITY OF OKLAHOMA HLTH SCIENCES CTR · PI LI, GUANGPU · 2006 to 2015
$2.4M
NIGMS NIH HHS GM074692NIGMS NIH HHS R01 GM074692
6 · The paper itself

Abstract

Rabex-5 is a guanine nucleotide exchange factor (GEF) for Rab5. Here, we report the identification of a novel functional domain of Rabex-5 that is essential for its membrane targeting and Rab5 GEF activity in vivo. The data show that full-length Rabex-5 efficiently activates Rab5 in the cell. However, the GEF domain itself (residues 135-399) is inactive in this respect, despite its activity in vitro. Generation and characterization of a series of Rabex-5 constructs reveal that the GEF domain is unable to target to early endosomes and that a sequence N-terminal to the GEF domain can restore its early endosomal targeting and its ability to activate Rab5 in the cell. This region (residues 81-135) is termed membrane-binding motif, which together with the downstream helical bundle domain (residues 135-230) forms an early endosomal targeting (EET) domain necessary and sufficient for association with early endosomes. Furthermore, several active Rabex-5 constructs do not contain the Rabaptin-5-binding domain in the C-terminal region. Thus, Rabex-5 can target to early endosomes via the EET domain and activate Rab5 in a Rabaptin-5-independent manner in vivo. We discuss a model to reconcile these in vivo data with previous in vitro results on Rabex-5 function and its interaction with Rabaptin-5.

Indexed as

AnimalsCattleCell MembraneCricetinaeEndosomesEnzyme ActivationGuanine Nucleotide Exchange FactorsMembrane FusionModels, BiologicalMutant ProteinsProtein BindingProtein Structure, TertiaryProtein Transportrab5 GTP-Binding ProteinsVesicular Transport ProteinsGuanine Nucleotide Exchange FactorsMutant Proteinsrab5 GTP-Binding ProteinsVesicular Transport Proteins

Identifiers

PMID17699593
PMCPMC1995700

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.