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RhoBTB1 interacts with ROCKs and inhibits invasion.

Raquel B Haga1, Ritu Garg1, Francesca Collu1

  • 1Randall Centre of Cell and Molecular Biophysics, King's College London, New Hunt's House, Guy's Campus, London SE1 1UL, U.K.

The Biochemical Journal
|August 22, 2019
PubMed
Summary
This summary is machine-generated.

RhoBTB1 protein suppresses prostate cancer invasion by interacting with ROCK1 and ROCK2. This interaction influences Cullin3 binding and protein degradation, impacting cell behavior.

Keywords:
Cullin3Rho GTPasesRho-kinasesRhoBTBcell invasionphosphorylation

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Cancer Research

Background:

  • RhoBTB1 is an atypical Rho GTPase with unique structural features.
  • Unlike other Rho GTPases, RhoBTB1's role in cytoskeletal dynamics and cell motility is not well-established.
  • Prostate cancer progression involves complex cellular mechanisms, including invasion and motility.

Purpose of the Study:

  • To investigate the function of RhoBTB1 in prostate cancer cell invasion.
  • To elucidate the molecular mechanisms underlying RhoBTB1's role in cancer progression.
  • To identify potential interactions between RhoBTB1 and other key regulatory proteins.

Main Methods:

  • Depletion of RhoBTB1 in prostate cancer cells.
  • Assessment of cell invasion and elongation in Matrigel.
  • Co-immunoprecipitation assays to study protein-protein interactions.
  • Site-directed mutagenesis to identify key amino acids involved in binding.
  • Analysis of RhoBTB1 phosphorylation and Cullin3 association.

Main Results:

  • RhoBTB1 depletion significantly increased prostate cancer cell invasion and induced cell elongation.
  • RhoBTB1 was found to associate with ROCK1 and ROCK2, with the Rho domain mediating ROCK1 interaction.
  • Specific amino acid mutations in the Rho domain affected RhoBTB1-ROCK1 binding.
  • RhoBTB1 is a substrate for ROCK1, and phosphorylation sites are crucial for Cullin3 association.
  • RhoBTB1 depletion reduced Cullin3 binding, suggesting a role in ubiquitin ligase complex regulation.

Conclusions:

  • RhoBTB1 acts as a suppressor of prostate cancer cell invasion.
  • The interaction between RhoBTB1 and ROCKs is critical for regulating RhoBTB1's association with Cullin3.
  • RhoBTB1 influences cancer cell invasion potentially through Cullin3-mediated protein degradation pathways.