Fig. 5
From: Association of activated Gαq to the tumor suppressor Fhit is enhanced by phospholipase Cβ
The chimera zα2β4 stimulates PLCβ but does not interact with Fhit. a Schematic representation of the zα2β4 and 16α2β4 chimeras. The linearized secondary structure of Gαq (filled with white) includes a helical domain (helices A-G) and a GTPase domain (helices 1–5 and strands 1–6). In the secondary structures of Gα16, Gαz, C128, zα2β4 or 16α2β4, the sequences from Gα16 are filled with black and those from Gαz are filled with gray. b Inositol phosphates accumulation assays were performed in COS-7 cells transfected with the wild-type or constitutively active mutants of Gα16, Gαz, C128, zα2β4 or 16α2β4. The relative IP3 production was quantified. The expressions of the chimeras were examined by the Western blot. * Gα16QL and zα2β4QL significantly increased the IP3 production (Dunnett’s t test, P < 0.05). c HEK293 cells were transiently co-transfected with Flag tagged Fhit and the wild-type or constitutively active mutants of Gα16, Gαz, zα2β4 or 16α2β4. Cell lysates were immunoprecipitated with anti-Flag agarose affinity gel (upper panels). Expression levels of Gα16, Gαz, Flag-Fhit and α-tubulin in the total cell lysate were detected by western blotting (lower panels)