complex(p(FPLX:"G_beta"), p(FPLX:"G_gamma"), p(HGNC:CHRNA7, var("p.345A"), var("p.346A"), var("p.347A"), var("p.348A")))

Components

• p(FPLX:"G_beta")
• p(FPLX:"G_gamma")
• p(HGNC:CHRNA7, var("p.345A"), var("p.346A"), var("p.347A"), var("p.348A"))

As shown in Fig. 3A, coupling between Gαq and α7 nAChRs was virtually abolished by expression of α7345–348A. A noticeable loss in Gαq (−62.18%) and Gβγ (−20.03%) expression within the α7 nAChR complex IP was seen in cells transfected with α7345–348A (Fig. 3A). PubMed:26088141

An increase in G protein association within the α7 complex was observed in α7+ cells (Gαq +16.71%; Gβγ +19.90%) (Fig. 3A). Similar findings in transfected N2a cells indicate a loss in G protein association within the α7 complex when α7345–348A nAChRs are expressed (Fig. 3B). PubMed:26088141

The data complements earlier findings on the ability of α7345–348A to function as a dominant negative blocker of G protein coupling in PC12 cells, and suggests that the GPBC directs nAChR association with Gαq and Gβγ. PubMed:26088141