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. Author manuscript; available in PMC: 2014 Nov 1.
Published in final edited form as: Cell Signal. 2013 Jul 17;25(11):2155–2162. doi: 10.1016/j.cellsig.2013.07.009

Fig. 2. The binding of arrestin-1 mutants to P-Rh and P-Rh* forms of WT and constitutively active M257Y rhodopsin does not depend on GRK subtype.

Fig. 2

A. Translated radiolabeled WT arrestin-1 (WT) and indicated mutants (100 fmol) were incubated with 0.3 μg of WT rhodopsin phosphorylated by indicated GRKs in the dark (P-Rh) or room light (P-Rh*) in 50 μl at 37°C for 5 min. The samples were cooled on ice, and bound arrestins were separated from free by gel-filtration on 2-ml Sephadex G-100 columns, as described in methods. Bound arrestins eluted with rhodopsin-containing HDL particles were quantified by scintillation counting. *, p<0.05, as compared to WT rhodopsin phosphorylated with GRK1 and GRK2. B. The same experiment described in A was performed with M257Y rhodopsin. Means ± SD of two independent experiments performed in duplicate are shown in both panels.