Evidence map›Paper›PMID 22628549›Full record

ArticleThe Journal of biological chemistry2012

Quantitative analysis of prenylated RhoA interaction with its chaperone, RhoGDI.

Zakir Tnimov, Zhong Guo, Yann Gambin, Uyen T T Nguyen, Yao-Wen Wu, Daniel Abankwa, Anouk Stigter, Brett M Collins, Herbert Waldmann, Roger S Goody and 1 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
2.0field-weighted citation impact, top 13% 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

31 citing papers in PubMed, 59 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Transient Structural Properties of the Rho GDP-Dissociation Inhibitor.Angewandte Chemie (International ed. in English) · 2024
    Article
  6. Article
  7. Article
  8. Article
  9. Crystal Structure ofBiology · 2022
    Article
  10. The Pseudo-Natural Product Rhonin Targets RHOGDI.Angewandte Chemie (International ed. in English) · 2022
    Article
  11. Electrostatic Forces Mediate the Specificity of RHO GTPase-GDI Interactions.International journal of molecular sciences · 2021
    Article
  12. Article
  13. Molecular subversion of Cdc42 signalling in cancer.Biochemical Society transactions · 2021
    Review
  14. Article
  15. Article
  16. Review
  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

11 authors at 4 institutions in 3 countries.

Zakir TnimovDepartment of Molecular Cell Biology, Institute for Molecular Bioscience, The University of Queensland, 306 Carmody Road, St. Lucia, Queensland 4072, Australia.
Zhong Guo
Yann Gambin
Uyen T T Nguyen
Yao-Wen Wu
Daniel Abankwa
Anouk Stigter
Brett M Collins
Herbert Waldmann
Roger S Goody
Kirill Alexandrov
University of Queensland · AUMax Planck Institute of Molecular Physiology · DEMax Planck Society · DETurku Centre for Biotechnology · FI

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Small GTPases of the Rho family regulate cytoskeleton remodeling, cell polarity, and transcription, as well as the cell cycle, in eukaryotic cells. Membrane delivery and recycling of the Rho GTPases is mediated by Rho GDP dissociation inhibitor (RhoGDI), which forms a stable complex with prenylated Rho GTPases. We analyzed the interaction of RhoGDI with the active and inactive forms of prenylated and unprenylated RhoA. We demonstrate that RhoGDI binds the prenylated form of RhoA·GDP with unexpectedly high affinity (K(d) = 5 pm). The very long half-life of the complex is reduced 25-fold on RhoA activation, with a concomitant reduction in affinity (K(d) = 3 nm). The 2.8-Å structure of the RhoA·guanosine 5'-[β,γ-imido] triphosphate (GMPPNP)·RhoGDI complex demonstrated that complex formation forces the activated RhoA into a GDP-bound conformation in the absence of nucleotide hydrolysis. We demonstrate that membrane extraction of Rho GTPase by RhoGDI is a thermodynamically favored passive process that operates through a series of progressively tighter intermediates, much like the one that is mediated by RabGDI.

Indexed as

Protein PrenylationAmino Acid SequenceBase SequenceCrystallizationDNA PrimersGuanine Nucleotide Dissociation InhibitorsHumansMolecular Sequence DataPolymerase Chain ReactionProtein BindingrhoA GTP-Binding Proteinrho Guanine Nucleotide Dissociation Inhibitor alpharho-Specific Guanine Nucleotide Dissociation InhibitorsSequence Homology, Amino AcidSpectrometry, FluorescenceSpectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationARHGDIA protein, humanDNA PrimersGuanine Nucleotide Dissociation InhibitorsrhoA GTP-Binding Proteinrho Guanine Nucleotide Dissociation Inhibitor alpharho-Specific Guanine Nucleotide Dissociation Inhibitors

Identifiers

PMID22628549
PMCPMC3410996
OpenAlexW2144641981

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.