Evidence map›Paper›PMID 31431478›Full record

ArticleThe Biochemical journal2019

RhoBTB1 interacts with ROCKs and inhibits invasion.

Raquel B Haga, Ritu Garg, Francesca Collu, Bárbara Borda D'Agua, Sofia T Menéndez, Audrey Colomba, Franca Fraternali, Anne J Ridley

Open access · hybridAbstract read
In one paragraph

Article in The Biochemical journal, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
0.7field-weighted citation impact, top 31% 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

14 citing papers in PubMed, 15 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Review
  6. Review
  7. Article
  8. Review
  9. Article
  10. Statins change the cytokine profile inFrontiers in immunology · 2022
    Article
  11. Article
  12. Review
  13. Article
  14. 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 at 1 institution in 1 country.

Raquel B HagaRandall Centre of Cell and Molecular Biophysics, King's College London, New Hunt's House, Guy's Campus, London SE1 1UL, U.K.
Ritu GargRandall Centre of Cell and Molecular Biophysics, King's College London, New Hunt's House, Guy's Campus, London SE1 1UL, U.K.
Francesca ColluRandall Centre of Cell and Molecular Biophysics, King's College London, New Hunt's House, Guy's Campus, London SE1 1UL, U.K.
Bárbara Borda D'AguaRandall Centre of Cell and Molecular Biophysics, King's College London, New Hunt's House, Guy's Campus, London SE1 1UL, U.K.
Sofia T MenéndezRandall Centre of Cell and Molecular Biophysics, King's College London, New Hunt's House, Guy's Campus, London SE1 1UL, U.K.
Audrey ColombaRandall Centre of Cell and Molecular Biophysics, King's College London, New Hunt's House, Guy's Campus, London SE1 1UL, U.K.
Franca FraternaliRandall Centre of Cell and Molecular Biophysics, King's College London, New Hunt's House, Guy's Campus, London SE1 1UL, U.K.
Anne J RidleyRandall Centre of Cell and Molecular Biophysics, King's College London, New Hunt's House, Guy's Campus, London SE1 1UL, U.K. anne.ridley@bristol.ac.uk.ORCID 0000-0001-8186-5708
King's College London · GB

Funding

Biotechnology and Biological Sciences Research CouncilCancer Research UK 15961Cancer Research UK C6620/A15961Medical Research Council
6 · The paper itself

Abstract

RhoBTB1 is an atypical Rho GTPase with two BTB domains in addition to its Rho domain. Although most Rho GTPases regulate actin cytoskeletal dynamics, RhoBTB1 is not known to affect cell shape or motility. We report that RhoBTB1 depletion increases prostate cancer cell invasion and induces elongation in Matrigel, a phenotype similar to that induced by depletion of ROCK1 and ROCK2. We demonstrate that RhoBTB1 associates with ROCK1 and ROCK2 and its association with ROCK1 is via its Rho domain. The Rho domain binds to the coiled-coil region of ROCK1 close to its kinase domain. We identify two amino acids within the Rho domain that alter RhoBTB1 association with ROCK1. RhoBTB1 is a substrate for ROCK1, and mutation of putative phosphorylation sites reduces its association with Cullin3, a scaffold for ubiquitin ligases. We propose that RhoBTB1 suppresses cancer cell invasion through interacting with ROCKs, which in turn regulate its association with Cullin3. Via Cullin3, RhoBTB1 has the potential to affect protein degradation.

Indexed as

AnimalsChlorocebus aethiopsCOS CellsCullin ProteinsHeLa CellsHumansMaleNeoplasm InvasivenessNeoplasm ProteinsPC-3 CellsProstatic Neoplasmsrho-Associated Kinasesrho GTP-Binding ProteinsCUL3 protein, humanCullin ProteinsNeoplasm Proteinsrho-Associated KinasesRhoBTB1 protein, humanrho GTP-Binding ProteinsROCK1 protein, humanROCK2 protein, humancell invasionCullin3phosphorylationRhoBTBRho GTPasesRho-kinases

Identifiers

PMID31431478
PMCPMC6744581
OpenAlexW2969369445

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.