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Fig. 2 | BMC Structural Biology

Fig. 2

From: An intact helical domain is required for Gα14 to stimulate phospholipase Cβ

Fig. 2

The putative PLCβ domain of Gα14 is not required for PLCβ interaction and activation. a Schematic representation of the 14z151, 203z14, 14z173, and 182z14 chimeras. Predicted secondary structures are illustrated as boxes (α helices) or circles (β strands) above the chimeras. Black areas represent human Gα14 sequence while those in grey signify the corresponding sequence of human Gαz. b HEK293 cells were co-transfected with PLCβ2 and the indicated Gα protein or chimeras. Cell lysates from the transfectants were immunoprecipitated by anti-PLCβ2 antiserum. The immunoprecipitates were immunoblotted with anti-Gα14, anti-Gαz or anti-PLCβ2 antiserum. Aliquots of cell lysates were used to detect the expression levels of Gα14, Gαz and PLCβ by Western blot analysis (TCL). Data shown represent one of three sets of immunoblots; two other sets yielded similar results. c HEK293 cells were transiently transfected with wild-type or constitutively active mutants (QL) of Gα protein or chimeras. Cells were then labelled and assayed for IP3 formation. Fold stimulations were calculated as the ratios of QL-induced to wild-type IP3 accumulations. Data represent the mean ± S.E.M. of three independent experiments, n = 3. *, IP3 production was significantly enhanced as compared to corresponding wild-type transfected cells; Dunnett t test, p < 0.05

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