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. 1998 Mar 3;95(5):2222–2226. doi: 10.1073/pnas.95.5.2222

Figure 3.

Figure 3

Phosphorylation of wild-type and mutant V2Rs. The phosphate incorporated into the proteins in response to 100 nM AVP was quantified in the immunoprecipitated receptors for the WT, 369t, 362t, and S363A mutant receptors. (A) Autoradiographic image of WT, 369t, and 362t phosphorylated V2Rs in a representative experiment. (B) Summary of the quantification of receptor phosphorylation. S363A V2R incorporated 88 ± 12%, 369t incorporated 60 ± 8%, and 362t incorporated 33 ± 7% of the phosphate incorporated by WT V2R. The values for each construct are expressed as percentage (mean ± SEM, n = 4) of the phosphate incorporated into the wild-type V2R after normalization for the number of binding sites detected with each construct.