The IκB kinase complex is required for plexin-B-mediated activation of RhoA

PLoS One. 2014 Aug 19;9(8):e105661. doi: 10.1371/journal.pone.0105661. eCollection 2014.

Abstract

Plexins are widely expressed transmembrane proteins that mediate the cellular effects of semaphorins. The molecular mechanisms of plexin-mediated signal transduction are still poorly understood. Here we show that signalling via B-family plexins leading to the activation of the small GTPase RhoA requires activation of the IκB kinase (IKK)-complex. In contrast, plexin-B-dependent regulation of R-Ras activity is not affected by IKK activity. This regulation of plexin signalling depends on the kinase activity of the IKK-complex, but is independent of NF-κB activation. We confirm that the IKK-complex is active in tumour cells and osteoblasts, and we demonstrate that plexin-B-dependent tumour cell invasiveness and regulation of osteoblast differentiation require an active IKK-complex. This study identifies a novel, NF-κB-independent function of the IKK-complex and shows that IKK directs plexin-B signalling to the activation of RhoA.

MeSH terms

  • Cell Adhesion Molecules / metabolism*
  • Cell Differentiation / genetics
  • Cell Line
  • Cell Line, Tumor
  • HEK293 Cells
  • Humans
  • I-kappa B Kinase / metabolism*
  • MCF-7 Cells
  • NF-kappa B / metabolism
  • Nerve Tissue Proteins / metabolism*
  • Signal Transduction / genetics
  • rhoA GTP-Binding Protein / metabolism*

Substances

  • Cell Adhesion Molecules
  • NF-kappa B
  • Nerve Tissue Proteins
  • plexin
  • I-kappa B Kinase
  • rhoA GTP-Binding Protein

Grants and funding

The authors received no specific funding for this work.