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Sci. Signal., 7 July 2009
[DOI: 10.1126/scisignal.2000444]

Supplementary Materials for:

Oxygen-Regulated β2-Adrenergic Receptor Hydroxylation by EGLN3 and Ubiquitylation by pVHL

Liang Xie, Kunhong Xiao, Erin J. Whalen, Michael T. Forrester, Robert S. Freeman, Guohua Fong, Steven P. Gygi, Robert J. Lefkowitz, and Jonathan S. Stamler*

*To whom correspondence should be addressed. E-mail: staml001{at}mc.duke.edu

This PDF file includes:

  • Fig. S1. Normoxia-stabilized HIF-1α (HIF-1αP402A/P564G) has no effect on β2AR abundance in β2AR-293 cells.
  • Fig. S2. β2AR colocalizes and interacts with endogenous pVHL.
  • Fig. S3. Tandem MS/MS spectra of peptide LLCEDLPGTEDFVGHQGTVPSDNIDSQGR and the corresponding proline-hydroxylated peptides OH-Pro382 and OH-Pro395.
  • Fig. S4. Mapping the interaction between β2AR and EGLN3.

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Format: Adobe Acrobat PDF

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Citation: L. Xie, K. Xiao, E. J.Whalen, M. T. Forrester, R. S. Freeman, G. Fong, S. P. Gygi, R. J. Lefkowitz, J. S. Stamler, Oxygen-Regulated β2-Adrenergic Receptor Hydroxylation by EGLN3 and Ubiquitylation by pVHL. Sci. Signal. 2, ra33 (2009).

© 2009 American Association for the Advancement of Science

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