RGS Proteins Maintain Robustness of GPCR-GIRK Coupling by Selective Stimulation of the G Protein Subunit Gα_o

Huai-hu Chuang* and Alexander Y. Chuang

*To whom correspondence should be addressed. E-mail: huai-hu.chuang{at}cornell.edu

This PDF file includes:

• Materials and Methods
• Mathematical simulation of G protein activation for Fig. 1A
• Membrane-targeted RGS constructs
• Fig. S1. Deactivation kinetics of A1 or m2 for various RGS proteins.
• Fig. S2. RGS4 does not stimulate β2-AR–stimulated Gα_s-dependent GIRK currents.
• Fig. S3. Deactivation kinetics of membrane-associated RGS box constructs.
• Fig. S4. Deactivation kinetics and ACh dose-response curves of oocytes with or without the full-length RGS4N128A.
• Fig. S5. Deactivation kinetics of the lyn-tagged R4Box and mutants.
• Fig. S6. Effects of PTX treatment.
• Fig. S7. RGS expression level–dependent deactivation kinetics.
• Fig. S8. Increased RGS8 expression enhanced the acceleration of deactivation kinetics.
• Fig. S9. GTP-γ-S induced GIRK activation in Gα_i1-expressing oocyte membranes.
• Fig. S10. RGS4 exhibited its GAP effect on Gα_i1 R178M.
• Table S1. P values for comparison of RGS effects on current enhancement in Fig. 1D.
• Table S2. P values for stimulatory effects on GIRK current by various membrane-targeted RGS box constructs.
• References
  

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© 2012 American Association for the Advancement of Science