Supplementary Materials

This PDF file includes:

• Fig. S1. Schematics of the assays used to characterize WT and mutant CXCR4 in this study.
• Fig. S2. A wide range of CXCR4 expression yields identical β-arrestin2 and Gα_i signaling parameters.
• Fig. S3. Total and cell surface expression of receptors with mutations of residues important for signaling as suggested by BRET experiments.
• Fig. S4. CXCR4 residues Glu²⁶⁸(ECL3) and Glu²⁷⁵(7.26) are not critical for CXCL12-mediated CXCR4 activation.
• Fig. S5. CRS1 is important for the potency but not the efficacy of CXCL12-mediated G protein engagement by CXCR4.
• Fig. S6. Predicted consequence of the binding of dimeric CXCL12 to CXCR4.
• Fig. S7. Signal amplification in Ca²⁺ mobilization experiments obscures mutation-induced defects.
• Table S1. Key predicted charge interactions in CRS1, CRS1.5, and CRS2 of the CXCR4-CXCL12 complex.
• Table S2. Previously published effects of CXCR4 mutations tested in this study.
• Table S3. Signaling parameters obtained from the β-arrestin2 and mini-Gα_i association BRET experiments.
• Table S4. Signaling parameters obtained from the Ca²⁺ mobilization experiments.
• References (79–84)

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