Lysophosphatidylinositol Induced Morphological Changes and Stress Fiber Formation through the GPR55-RhoA-ROCK Pathway

Int J Mol Sci. 2022 Sep 18;23(18):10932. doi: 10.3390/ijms231810932.

Abstract

We previously reported that lysophosphatidylinositol (LPI) functions as an endogenous agonist of GPR55, a novel cannabinoid receptor. However, the physiological roles of LPI-GPR55 have not yet been elucidated in detail. In the present study, we found that LPI induced morphological changes in GPR55-expressing HEK293 cells. LPI induced the cell rounding of GPR55-expressing HEK293 cells but not of empty-vector-transfected cells. LPI also induced the activation of small GTP-binding protein RhoA and increased stress fiber formation in GPR55-expressing HEK293 cells. The inhibition of RhoA and Rho kinase ROCK by the C3 exoenzyme and the ROCK inhibitor reduced LPI-induced cell rounding and stress fiber formation. These results clearly indicated that the LPI-induced morphological changes and the assembly of the cytoskeletons were mediated through the GPR55-RhoA-ROCK pathway.

Keywords: G12/13-RhoA-ROCK pathway; GPR55; endocannabinoid; lysophosphatidylinositol; lysophospholipid mediator; morphological change.

MeSH terms

  • HEK293 Cells
  • Humans
  • Lysophospholipids / metabolism
  • Receptors, Cannabinoid / metabolism
  • Receptors, G-Protein-Coupled* / agonists
  • Stress Fibers / metabolism
  • rho-Associated Kinases* / metabolism
  • rhoA GTP-Binding Protein / genetics
  • rhoA GTP-Binding Protein / metabolism

Substances

  • GPR55 protein, human
  • Lysophospholipids
  • Receptors, Cannabinoid
  • Receptors, G-Protein-Coupled
  • lysophosphatidylinositol
  • RHOA protein, human
  • rho-Associated Kinases
  • rhoA GTP-Binding Protein