There was an error published in J. Cell Sci.127, 2697-2708.

In Fig. 2, the V1C1 western blot was inadvertently duplicated in panels A and B. The V1C1 western blot has been replaced with the correct image in panel B 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.

Fig. 2.

RILP modulates V1G1 abundance in HeLa cells through ubiquitylation-dependent proteasomal degradation. (A) Lysates of control HeLa cells (NT) or cells expressing HA–RILP were subjected to western blot analysis using primary antibodies against V1G1, HA, V1C1, V0D1 and tubulin. (B) Cells treated with control siRNA (scr), RILP-specific siRNA (RILPi) or V1G1-specific siRNA (V1G1i) were subjected to western blot analysis using primary antibodies against V1G1, RILP, V1C1, V0D1 and tubulin. (C) Lysates of control HeLa cells or cells expressing HA–RILP, HA–RILPΔC2 or HA–RILPC33 were subjected to western blot analysis using anti-V1G1, anti-HA and anti-tubulin antibodies. (D) Cells treated with control siRNA or RILP-specific siRNA and transfected with HA–RILP, as indicated, were subjected to western blot analysis using anti-V1G1, anti-RILP and anti-tubulin antibodies. (E–G) Real-time PCR was performed on control HeLa cells, or cells expressing HA–RILP (RILP1 and RILP2) or silenced for RILP (RILPi1 and RILPi2), and the amount of RILP (E,F) or of V1G1 (G) was quantified relative to the control GAPDH RNA transcript. (H) Control cells or cells expressing HA–RILP, as indicated, were either untreated or treated with the proteasomal inhibitor MG132. Lysates were then subjected to western blot analysis with antibodies against V1G1, HA and tubulin. (I) Control cells or cells transfected with HA–V1G1 and RILP, as indicated, were either untreated or treated with MG132. Lysates were subjected to western blot analysis using antibodies against RILP, V1G1 and tubulin, and to immunoprecipitation using an anti-HA antibody. Immunoprecipitates were subjected to western blot analysis using an anti-ubiquitin antibody.

Fig. 2.

RILP modulates V1G1 abundance in HeLa cells through ubiquitylation-dependent proteasomal degradation. (A) Lysates of control HeLa cells (NT) or cells expressing HA–RILP were subjected to western blot analysis using primary antibodies against V1G1, HA, V1C1, V0D1 and tubulin. (B) Cells treated with control siRNA (scr), RILP-specific siRNA (RILPi) or V1G1-specific siRNA (V1G1i) were subjected to western blot analysis using primary antibodies against V1G1, RILP, V1C1, V0D1 and tubulin. (C) Lysates of control HeLa cells or cells expressing HA–RILP, HA–RILPΔC2 or HA–RILPC33 were subjected to western blot analysis using anti-V1G1, anti-HA and anti-tubulin antibodies. (D) Cells treated with control siRNA or RILP-specific siRNA and transfected with HA–RILP, as indicated, were subjected to western blot analysis using anti-V1G1, anti-RILP and anti-tubulin antibodies. (E–G) Real-time PCR was performed on control HeLa cells, or cells expressing HA–RILP (RILP1 and RILP2) or silenced for RILP (RILPi1 and RILPi2), and the amount of RILP (E,F) or of V1G1 (G) was quantified relative to the control GAPDH RNA transcript. (H) Control cells or cells expressing HA–RILP, as indicated, were either untreated or treated with the proteasomal inhibitor MG132. Lysates were then subjected to western blot analysis with antibodies against V1G1, HA and tubulin. (I) Control cells or cells transfected with HA–V1G1 and RILP, as indicated, were either untreated or treated with MG132. Lysates were subjected to western blot analysis using antibodies against RILP, V1G1 and tubulin, and to immunoprecipitation using an anti-HA antibody. Immunoprecipitates were subjected to western blot analysis using an anti-ubiquitin antibody.

The authors apologise to the readers for any confusion that this error might have caused.