Activated heterotrimeric G protein α_i subunits inhibit Rap-dependent cell adhesion and promote cell migration.

ABSTRACT: Our recent work uncovered novel roles for activated Gα_i signaling in the regulation of neutrophil polarity and adhesion. Gα_iGTP-mediated enhancement of neutrophil polarization was dependent on inhibition of cAMP/PKA signaling, whereas reversal of Gβγ-stimulated adhesion was cAMP/PKA independent. To uncover the mechanism for Gα_i regulation of adhesion, we analyzed the effects of constitutively active Gα_i1(Q204L) expression on adhesion driven by constitutively active Rap1a(G12V) or its downstream effector Radil in neutrophil-like HL-60 cells, or in HT-1080 fibrosarcoma cells. In HT-1080 cells, Rap1a(G12V) or Radil cause an increase in cell spreading and adhesion to fibronectin, which are both reversed by Gα_i1(Q204L) but not WT Gα_i1<

SUBMITTER: To JY 

PROVIDER: S-EPMC5798289 | biostudies-literature | 2018 Feb

REPOSITORIES: biostudies-literature