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Figure 3


Fig. 3. Co-immunoprecipitation of effectors with Gß{gamma}. HEK 293 cells expressing the indicated proteins were dissolved in RIPA before immunoprecipitation. Precipitated proteins were separated on SDS-polyacrylamide gels and transferred to nitrocellulose for western blotting. (A) AC-RLuc was precipitated by anti-GFP antibodies from cells co-expressing GFP-Gß1 and G{gamma}2 (left panel). No detectable RLuc was precipitated if the cells also expressed untagged Gß1 (middle panel) or if they expressed RLuc in place of AC-RLuc (right panel). (B) HA-tagged Kir3.1 was precipitated with anti-Flag antibodies from cells co-expressing Flag-tagged Gß1 and wild-type G{gamma}2. Precipitation of a HA-tagged protein required co-expression of both Kir3.1-HA and Flag-Gß1. Solid arrows represent differentially glycosylated forms of Kir3.1 as seen in native tissues (Krapivinsky et al., 1995). Middle panel shows cell lysates blotted for expression of HA-tagged Kir3.1. Lower panel shows immunoprecipitation of Gß by anti-Flag antibodies. Open arrow indicates specific Gß signal. The blots are representative of at least three independent experiments.





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