Distinct Phosphorylation Sites on the β₂-Adrenergic Receptor Establish a Barcode That Encodes Differential Functions of β-Arrestin

Kelly N. Nobles, Kunhong Xiao,* Seungkirl Ahn, Arun K. Shukla, Christopher M. Lam, Sudarshan Rajagopal, Ryan T. Strachan, Teng-Yi Huang, Erin A. Bressler, Makoto R. Hara, Sudha K. Shenoy, Steven P. Gygi, Robert J. Lefkowitz*

*To whom correspondence should be addressed. E-mail: lefko001{at}receptor-biol.duke.edu (R.J.L.); khxiao{at}receptor-biol.duke.edu (K.X.)

This PDF file includes:

• Fig. S1. Endogenous GRK2 and 6 in HEK293 cells.
• Fig. S2. Specific β-arrestin2 recruitment to the β₂AR.
• Fig. S3. Overview of β₂AR phosphorylation analysis by MS-based quantitative proteomics.
• Fig. S4. Dephosphorylation of β₂AR Ser²⁴⁶ by isoproterenol stimulation.
• Fig. S5. Phosphorylation of Ser³⁵⁵/Ser³⁵⁶ on β₂AR as detected by LC-MS/MS and Western blotting.
• Fig. S6. Western blot analysis of phosphorylation of β₂AR on Ser³⁵⁵/Ser³⁵⁶ in response to isoproterenol and carvedilol stimulation.
• Fig. S7. Western blot analysis of β₂AR phosphorylation at Ser³⁹⁶, Ser⁴⁰⁷/Ser⁴¹¹, Ser²⁶¹/Ser²⁶², and Ser³⁴⁵/Ser³⁴⁶.
  

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