There was an error published in J. Cell Sci. 128, .
In Fig. 2, the HA–importin-α3 immunoprecipitation and corresponding Flag–NLS blots were inadvertently duplicated as the HA–importin-α5 immunoprecipitation and corresponding Flag–NLS blots. The two HA–importin-α5 blots have been replaced with the correct images in panel D in the figure shown below. There are no changes to the figure legend, which is accurate. This error does not affect the conclusions of the study.
The hTERT NLS interacts physically with importin α. (A) GST–importin-α1, GST–importin-α3, GST–importin-α5 and GST–importin-β1 were affinity purified and incubated with lysates that had been prepared from cells expressing Flag–NLS or Flag–S227A/7A, followed by immunoblotting with anti-Flag antibody. The purified GST fusion proteins were visualized by Coomassie staining and are indicated with arrowheads. Molecular mass makers are shown in kDa. (B) GST–NLS and GST–S227A/7A were purified and incubated with lysates prepared from cells expressing HA–importin-α1, HA–importin-α3, HA–importin-α5 and HA–importin-β1; the HA-tagged proteins were then detected. HA-tagged importin proteins are indicated with arrowheads. The purified GST fusion proteins were visualized by Coomassie staining. (C) MCF7 cells that had been transfected with Flag–NLS and either HA–importin-α proteins or HA–importin-β1 were subjected to immunoprecipitation (IP) with anti-Flag antibody, followed by immunoblotting with anti-HA antibody. HA-tagged importin proteins are indicated with arrowheads. (D) MCF7 cells transfected with Flag–NLS, HA–importin-α proteins and HA–importin-β1 were subjected to immunoprecipitation with anti-Flag antibody, followed by immunoblotting with anti-HA antibody. (E) MCF7 cells were subjected to immunoprecipitation with an anti-hTERT antibody; the immunoprecipitates were then probed for endogenous importin-α proteins and importin-β1. IgG antibody was used as a negative control. In B,C,D, asterisks mark the position of nonspecific immunoglobulin chains.
The hTERT NLS interacts physically with importin α. (A) GST–importin-α1, GST–importin-α3, GST–importin-α5 and GST–importin-β1 were affinity purified and incubated with lysates that had been prepared from cells expressing Flag–NLS or Flag–S227A/7A, followed by immunoblotting with anti-Flag antibody. The purified GST fusion proteins were visualized by Coomassie staining and are indicated with arrowheads. Molecular mass makers are shown in kDa. (B) GST–NLS and GST–S227A/7A were purified and incubated with lysates prepared from cells expressing HA–importin-α1, HA–importin-α3, HA–importin-α5 and HA–importin-β1; the HA-tagged proteins were then detected. HA-tagged importin proteins are indicated with arrowheads. The purified GST fusion proteins were visualized by Coomassie staining. (C) MCF7 cells that had been transfected with Flag–NLS and either HA–importin-α proteins or HA–importin-β1 were subjected to immunoprecipitation (IP) with anti-Flag antibody, followed by immunoblotting with anti-HA antibody. HA-tagged importin proteins are indicated with arrowheads. (D) MCF7 cells transfected with Flag–NLS, HA–importin-α proteins and HA–importin-β1 were subjected to immunoprecipitation with anti-Flag antibody, followed by immunoblotting with anti-HA antibody. (E) MCF7 cells were subjected to immunoprecipitation with an anti-hTERT antibody; the immunoprecipitates were then probed for endogenous importin-α proteins and importin-β1. IgG antibody was used as a negative control. In B,C,D, asterisks mark the position of nonspecific immunoglobulin chains.
The authors apologise to the readers for any confusion that this error might have caused.
