Evidence map›Paper›PMID 17450153›Full record

ArticleNature structural & molecular biology2007

Structural basis for Rab GTPase activation by VPS9 domain exchange factors.

Anna Delprato, David G Lambright

Open access · greenAbstract read
In one paragraph

Article in Nature structural & molecular biology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 78 papers.

0numbers the graph read from it
0cells of the map it votes in
78citing papers in PubMed
4.0field-weighted citation impact, top 6% 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

78 citing papers in PubMed, 143 citations in OpenAlex.

  1. Article
  2. ESCRTing the RABs through conversion.Biochemical Society transactions · 2025
    Review
  3. Article
  4. Article
  5. Rab21 recruits EEA1 and competes with Rab5 for Rabex-5 activation.Frontiers in cell and developmental biology · 2025
    Article
  6. Article
  7. Article
  8. Structural basis for Rab6 activation by the Ric1-Rgp1 complex.bioRxiv : the preprint server for biology · 2024
    Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Ras and Rab Interactor 3: From Cellular Mechanisms to Human Diseases.Frontiers in cell and developmental biology · 2022
    Review
  14. Review
  15. Crystal structure of a guanine nucleotide exchange factor encoded by the scrub typhus pathogenProceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  16. Crystal structure of the GDP-bound GTPase domain of Rab5a from Leishmania donovani.Acta crystallographica. Section F, Structural biology communications · 2020
    Article
  17. Article
  18. 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
  19. Article
  20. Article

18 more citing papers are in PubMed but not listed here.

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

2 authors at 1 institution in 1 country.

Anna DelpratoProgram in Molecular Medicine and Department of Biochemistry & Molecular Pharmacology, University of Massachusetts Medical School, Two Biotech, 373 Plantation Street, Worcester, Massachusetts 01605, USA.
David G Lambright
University of Massachusetts Chan Medical School · US

Funding

SUBCELLULAR LOCALIZATION OF PI 3-KINASE SIGNALINGP01DK060564 · NIDDK · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI FOGARTY, KEVIN EDWARD · 2001 to 2011
$13.9M
STRUCTURAL BASIS OF G PROTEIN MEDIATED SIGNALINGR01GM056324 · NIGMS · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI LAMBRIGHT, DAVID G · 1998 to 2018
$6.2M
NIDDK NIH HHS DK60564NIDDK NIH HHS P01 DK060564NIGMS NIH HHS GM56324NIGMS NIH HHS R01 GM056324
6 · The paper itself

Abstract

RABEX-5 and other exchange factors with VPS9 domains regulate endocytic trafficking through activation of the Rab family GTPases RAB5, RAB21 and RAB22. Here we report the crystal structure of the RABEX-5 catalytic core in complex with nucleotide-free RAB21, a key intermediate in the exchange reaction pathway. The structure reveals how VPS9 domain exchange factors recognize Rab GTPase substrates, accelerate GDP release and stabilize the nucleotide-free conformation. We further identify an autoinhibitory element in a predicted amphipathic helix located near the C terminus of the VPS9 domain. The autoinhibitory element overlaps with the binding site for the multivalent effector RABAPTIN-5 and potently suppresses the exchange activity of RABEX-5. Autoinhibition can be partially reversed by mutation of conserved residues on the nonpolar face of the predicted amphipathic helix or by assembly of the complex with RABAPTIN-5.

Indexed as

Binding SitesCrystallography, X-RayEnzyme ActivationGuanine Nucleotide Exchange FactorsGuanosine DiphosphateHumansMutationProtein Conformationrab GTP-Binding ProteinsVesicular Transport ProteinsGuanine Nucleotide Exchange FactorsGuanosine DiphosphateRAB22A protein, humanRABEP1 protein, humanRABGEF1 protein, humanrab GTP-Binding ProteinsVesicular Transport Proteins

Identifiers

PMID17450153
PMCPMC2254184
OpenAlexW2128506555

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.