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C. J. Abrams, N. W. Davies, P. A. Shelton and P. R. Stanfield

Journal of Physiology 493, 643-649 (1996)

On checking the sequences of the Kir2.1 contructs, we found that an additional mutation at postion 165 had been overlooked in the constuct we believed to be D172N. The bases found for the relevant codon were TTA, encoding leucine at position 165 rather than the serine residue which is found in wild-type channels. Thus the construct used was in fact S165L/D172N.

We examined the properties of the correct D172N. Rb⁺ continued to block D172N in a voltage-dependent manner, the block initially increasing with hyperpolarization before being relieved at negative voltages. Further, Rb⁺ currents were smaller than K⁺ currents, unlike the result shown in Fig. 2 (for S165L/D172N), where Rb⁺ permeated more rapidly at negative voltages than did K⁺. Similarly, Cs⁺ continued to block D172N in a steeply voltage-dependent manner, much as in wild-type.

Accordingly, we withdraw the conclusion of our paper that: 'Hand-in-hand with strong inward rectification is strong selectivity against Rb⁺, and ... the same Asp residues (D172) confer this selectivity'.

The same construct (S165L/D172N) was used in work described by Stanfield et al. (1994: Journal of Physiology 478, 1-6), but the error does not materially affect the results or conclusions of that paper. We thank Dr M. L. Leyland for bringing this error to our attention.

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