Supplementary Materials

Supplementary Materials for:

A calcium-sensing receptor mutation causing hypocalcemia disrupts a transmembrane salt bridge to activate β-arrestin–biased signaling

Caroline M. Gorvin, Valerie N. Babinsky, Tomas Malinauskas, Peter H. Nissen, Anders J. Schou, Aylin C. Hanyaloglu, Christian Siebold, E. Yvonne Jones, Fadil M. Hannan,* Rajesh V. Thakker*

*Corresponding author. Email: rajesh.thakker{at}ndm.ox.ac.uk (R.V.T.); fadil.hannan{at}liverpool.ac.uk (F.M.H.)

This PDF file includes:

  • Fig. S1. Plasma membrane and cytoplasmic CaSR in HEK293 cells.
  • Fig. S2. Abundance of CaSR in plasma membrane fractions.
  • Fig. S3. ERK phosphorylation in the ADH1-associated R680G and L173F mutant CaSRs used for densitometry analysis.
  • Fig. S4. siRNA-mediated knockdown of β-arrestin1 and β-arrestin2.
  • Fig. S5. Effect of NPS-2143 on β-arrestin–mediated MAPK signaling after stimulation with 10 mM [Ca2+]e.
  • Fig. S6. Effect of the engineered mutants E767R and E837R CaSRs on MAPK signaling.
  • Fig. S7. ERK phosphorylation in engineered E767R and E837R CaSR mutants used for densitometry analysis.
  • Fig. S8. Analysis of the CaSR Glu837 residue by homology modeling using the structure of mGluR1.
  • Fig. S9. Western blots to assess ERK phosphorylation in the engineered Glu680-Arg767 double CaSR mutant used for densitometry analysis.
  • Table S1. Clinical and biochemical findings in the parents and proband with the R680G CaSR mutation.

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