Jun dimerization protein 2 is a critical component of the Nrf2/MafK complex regulating the response to ROS homeostasis

Citation: Cell Death and Disease (2014) 5, e1344; doi:10.1038/cddis.2014.322

& 2014 Macmillan Publishers Limited All rights reserved 2041-4889/14 http://www.nature.com/cddis

Web End =www.nature.com/cddis

Corrigendum

Jun dimerization protein 2 is a critical component of the Nrf2/MafK complex regulating the response to ROS homeostasis

S Tanigawa, CH Lee, CS Lin, CC Ku, H Hasegawa, S Qin, A Kawahara, Y Korenori, K Miyamori, M Noguchi, LH Lee, YC Lin, CL Steve Lin, Y Nakamura, C Jin, N Yamaguchi, R Eckner, D-X Hou and KK Yokoyama

Cell Death and Disease (2014) 5, e1344; doi:http://dx.doi.org/10.1038/cddis.2014.322

Web End =10.1038/cddis.2014.322 ; published online 17 July 2014

Correction to: Cell Death and Disease (2013) 4, e921; doi:http://10.1038/cddis.2013.448

Web End =10.1038/cddis.2013.448 ; published online 14 November 2013

Since the publication of this paper, the authors have noticed that there was an error in Figure 2a. The western blotting

image was incorrect. The error has now been rectied. The corrected article appears online together with this corrigendum. The authors would like to apologize for any inconvenience this may have caused.

Corrigendum

2

10

WT Jdp2 KO

Jdp2 MafK

Nrf2 HO-1

NQO1 [afii9825]-Tubulin

10

Relative luciferase activity (fold)

Relative luciferase activity (fold)

Nrf2 (ng)

WT Jdp2 KO

WT

Jdp2 KO

8

8

6

6

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0 0 0.5 1 2 6 12 24 0 10 20 100

50

48

TPA (h)

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2.0

Jdp2 KO

TPA (-)

WT

6

Jdp2 KO

Relative luciferase activity (fold)

Relative luciferase activity (fold)

1.5

5

**

4

1.0

3

**

2

**

0.5

1

** **

**

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Nrf2 (ng) -

- -

- NS

Nrf2

50 50

50

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0.0

siRNA -

NS

Nrf2

Jdp2

Jdp2 (ng)

50

1 2 4

3

1 2 4

3

WT

Jdp2 KO

Flag

Jdp2 (#176)

Nrf2

Jdp2

IgG

1 2 3 1 2 3

+ NS + NS

[afii9826]-actin

[afii9826]-actin

siRNA

Figure 2 JDP2 is required for ARE activation. (a) Protein detection in WT and Jdp2 KO MEFs using western blotting. The cellular lysates from WT and Jdp2 KO MEFs (40 mg) were separated on SDS-PAGE and then transferred onto a membrane. Jdp2, MafK, Nrf2, HO-1, NQO1 and a-tubulin were immunodetected using specic antibodies.

(b) Relative NQO1 promoter activity in WT and Jdp2 KO MEFs in the presence of TPA at the indicated exposure times. After 24 h of culture, TPA (106 M) was added,

transfectants with pGL4hQR25luciferase were incubated for an additional 48 h and luciferase activity was measured (n 3) as described in Materials and Methods.

(c) Effect of Nrf2 on NQO1 promoter activity. pGL4hQR25luciferase (400 ng) plus 0100 ng of pcDNA3Nrf2 were transfected into WT and Jdp2 KO MEFs (5 104). One

day after transfection, cells were collected and luciferase activity was measured. Values from a representative experiment are given as meanS.D. (n 3). (d) Effect of JDP2

on ARE activity in the presence of Nrf2. Jdp2 KO MEFs (5 104) was transfected with 400 ng of pGL4hQR25luciferase, 50 ng of FLAG_SNrf2 and pcDNAJdp2,

respectively, as indicated. One day after transfection, cells were collected and luciferase activity was measured (n 3). **Po0.01. (e) Protein detection of FLAGNrf2 and

JDP2 in WT and Jdp2 KO MEFs using western blotting. The cellular lysates from WT and Jdp2 KO MEFs (40 mg) were separated on SDS-PAGE and then transferred onto a membrane. FLAG, Jdp2 and b-actin were immunodetected using specic antibodies, which were described in Materials and Methods. Lane number corresponded to each lane in d. (f) Effect of siRNA specic for Nrf2 and Jdp2 on ARE activity. WT and Jdp2 KO MEFs (5 104 cells) were transfected with 30 pmol of siRNA specic for Nrf2 or Jdp2

and 200 ng of pGL4hQR25luciferase plasmid as described in the text. After exposure for 30 h, luciferase activity was measured (n 3). The same amount of nonspecic

double-stranded RNA was used as a negative control (NS). **Po0.01. (g) Inhibition of the expression of Nrf2 and Jdp2 proteins by siRNA. WT and Jdp2 KO MEFs (5 104)

were transfected with 30 pmol of active siRNA and the control siRNA, together with reporter plasmids. After treatment for 30 h, cell extracts were analyzed by immunoblotting using Nrf2, Jdp2, IgG or b-actin antibodies. Lane 1, without siRNA; lane 2, with siRNA; and lane 3, with NS siRNA

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