In this Article, there are several instances where all-trans-retinal is incorrectly referred to as all-trans-retinol and all-trans-retinol is incorrectly abbreviated to ATR. The following sentences, and the revised figure below, are correct. In the abstract: Here we show that rod arrestin induces uptake of the agonist all-trans-retinal in only half the population of phosphorylated opsin in the native membrane. In the abstract: Such a mechanism would protect the rod cell in bright light by concurrently sequestering toxic all-trans-retinal and allowing regeneration with 11-cis-retinal. In the Results: Incidentally, both all-trans-retinol and beta-ionone also induced arrestin binding to OpsP with an apparent Kd ∼40 times higher than that for ATR (Fig. 3e). On the x axis of Fig. 3a: All-trans-retinal. In the legend to Fig. 3e: All-trans-retinol and beta-ionone were titrated against 4 μM arrestin+4 μM OpsP (100% phosphorylated) in isotonic buffer, and arrestin binding was measured by pull down. In the legend to Fig. 4: All-trans-retinol formation after addition of NADPH to samples of OpsP (2 μM) and ATR (4 μM) was monitored in the absence (dark red) or presence of 2 μM unlabelled arrestin (red). Experiments were performed in 50 mM HEPES buffer pH 7 without salt, 35 °C. In the legend to Table 1: ATR, all-trans-retinal; NA, not applicable; OpsP, phosphorylated opsin. The correct version of Fig. 3 and its legend follows.
The online version of the original article can be found at 10.1038/ncomms2000
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Sommer, M., Hofmann, K. & Heck, M. Erratum: Distinct loops in arrestin differentially regulate ligand binding within the GPCR opsin. Nat Commun 3, 1273 (2012) doi:10.1038/ncomms2284