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. Author manuscript; available in PMC: 2019 Mar 1.
Published in final edited form as: Cell Rep. 2018 Nov 27;25(9):2497–2509.e4. doi: 10.1016/j.celrep.2018.11.008

Figure 2. β-Arrestins Bind Melanopsin upon Light Activation and Participate in Its Deactivation.

Figure 2.

(A) Mouse Opn4 mutants carrying alanine (A) at candidate Ser/Thr (S/T) phosphorylation sites.

(B–F) In thisβ-galcomplementation assay (see Figure S1B), light-activated (5 min white light, 100 lx, red and blue bars) full-length Opn4 (WT) produces a robust chemiluminescent signal from OPN4-β-arrestin interaction compared to the dark control (black bars), while various phosphorylation-deficient Opn4 mutants show reduced barr1 or barr2 interaction (B) (2 way ANOVA, Bonferroni posthoc tests, *p < 0.05, ***p < 0.001, ns p > 0.05). Attenuation of melanopsin photoresponse in CHO cells transduced with either Opn4WT or Opn49A and βArr1, βArr2, or their constitutively active mutant βarr1R169E and βarr2R170E: average traces (C and D, respectively) and average peak amplitude (E) and time (F) (seconds ± SEMs) for the peak response to return to 5% of maximal response (n = 12–14, Student’s t test).