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Table 1 Functional characterizations of the chimeras and their correlation with intact PLCβ or Gα14 helical domains

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

  PLCβ stimulation Adenylyl cyclase inhibition PLCβ interaction TPR1 interaction Intact PLCβ domain Intact Gα14 helical domain
Gα14 Yes No Yes Yes Yes Yes
203z14 No No No Yes Yes No
14z151 Yes No Yes Yes No Yes
182z14 No No No Yes Yes No
14z173 Yes No Yes Yes No Yes
14β2β3 No Yes No No No No
zβ2β3 Yes No Yes Yes Yes Yes
14z224 No Yes No Yes No No
131z14 No No No Yes Yes No
14αDEF No Yes No Yes No No
zαDEF No No No No Yes No
14α2β4α3 No Yes No Yes No No
zα2β4α3 Yes No Yes Yes No Yes
14αN No Yes No No No No
zαN Yes No Yes Yes Yes Yes
Gαz No Yes No No No No
  1. Results of Gα proteins and chimeras in functional studies and co-immunoprecipitation assays are summarized. PLCβ stimulation was determined by measuring IP3 production by constitutively active (QL) chimeras as compared to their corresponding wild type activity (Figs. 2c, 3c, 4c, and 5c). The ability of QL-chimeras to inhibit adenylyl cyclase was determined in FSK-induced cAMP accumulation assays (Fig. 6a). Co-immunoprecipitation assays were performed using anti-PLCβ2 and anti-FLAG for the detection of PLCβ (Figs. 2b, 3b, 4b, and 5c) and TPR1 (Fig. 6b), respectively. Constructs containing an intact PLCβ binding domain (α2-β4-α3-β5 region) or an intact helical domain (αA-αF region) of Gα14 are also shown
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BMC Structural Biology

ISSN: 1472-6807

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