Literature DB >> 30240415

Correction: FAS-associated factor-1 positively regulates type I interferon response to RNA virus infection by targeting NLRX1.

Jae-Hoon Kim, Min-Eun Park, Chamilani Nikapitiya, Tae-Hwan Kim, Md Bashir Uddin, Hyun-Cheol Lee, Eunhee Kim, Jin Yeul Ma, Jae U Jung, Chul-Joong Kim, Jong-Soo Lee.   

Abstract

[This corrects the article DOI: 10.1371/journal.ppat.1006398.].

Entities:  

Year:  2018        PMID: 30240415      PMCID: PMC6150512          DOI: 10.1371/journal.ppat.1007302

Source DB:  PubMed          Journal:  PLoS Pathog        ISSN: 1553-7366            Impact factor:   6.823


The authors would like to correct Fig 5. In Fig 5A, the β-actin panel was duplicated from the β-actin panel in Fig 5B. Additionally, in Fig 5B, the Phospho-TBK1 panel was edited incorrectly. These errors occurred during composition of the final figure and the authors now provide corrected version of Fig 5.
Fig 5

FAF1 activates the type I IFN signaling pathway and induces IFN-related gene expression.

(A and B) Control RAW264.7 (RAW-Scramble) and FAF1 knockdown RAW264.7 (RAW-sh-FAF1) cells (A) or control RAW264.7 (RAW-Control) and FAF1-overexpressing RAW264.7 (RAW-FAF1) cells (B) were infected with PR8-GFP (MOI = 2). At the indicated time points after infection, phosphorylated IRF3, p65, STAT1, p38 and TBK1, and total IRF3, p65 and STAT1 were measured in cell extracts by immunoblotting. β-actin was used to confirm equal loading of proteins. (C and D) Wild-type MEFs (MEF/FAF1+/+) and FAF1 knockdown MEFs (MEF/FAF1gt/gt) (C) and BMDMs isolated from FAF1+/+ (BMDM/FAF1+/+) and FAF1gt/gt (BMDM/FAF1gt/gt) mice (D) were infected with PR8-GFP (MOI = 1 and 3, respectively) for 12 hr, followed by total RNA extraction. Expression of mRNA encoding IFN-β, IFN-α, PKR, OAS, OAS-1β, MX-1, ISG-15, ISG-56, ADAR1 and IL-6 for MEFs and IFN-β, PKR, OAS, OAS-1β, MX-1, ISG-15, ISG-20, ISG-56, ADAR1 and IL-6 for BMDMs was analyzed by qRT-PCR. Data are presented as the mean ± SEM. Data are representative of at least two independent experiments.

FAF1 activates the type I IFN signaling pathway and induces IFN-related gene expression.

(A and B) Control RAW264.7 (RAW-Scramble) and FAF1 knockdown RAW264.7 (RAW-sh-FAF1) cells (A) or control RAW264.7 (RAW-Control) and FAF1-overexpressing RAW264.7 (RAW-FAF1) cells (B) were infected with PR8-GFP (MOI = 2). At the indicated time points after infection, phosphorylated IRF3, p65, STAT1, p38 and TBK1, and total IRF3, p65 and STAT1 were measured in cell extracts by immunoblotting. β-actin was used to confirm equal loading of proteins. (C and D) Wild-type MEFs (MEF/FAF1+/+) and FAF1 knockdown MEFs (MEF/FAF1gt/gt) (C) and BMDMs isolated from FAF1+/+ (BMDM/FAF1+/+) and FAF1gt/gt (BMDM/FAF1gt/gt) mice (D) were infected with PR8-GFP (MOI = 1 and 3, respectively) for 12 hr, followed by total RNA extraction. Expression of mRNA encoding IFN-β, IFN-α, PKR, OAS, OAS-1β, MX-1, ISG-15, ISG-56, ADAR1 and IL-6 for MEFs and IFN-β, PKR, OAS, OAS-1β, MX-1, ISG-15, ISG-20, ISG-56, ADAR1 and IL-6 for BMDMs was analyzed by qRT-PCR. Data are presented as the mean ± SEM. Data are representative of at least two independent experiments. The authors confirm that these changes do not alter their findings. The authors have provided raw, uncropped blots as Supporting Information.

Raw data for Fig 5A.

Control RAW264.7 (Scramble) and FAF1 knockdown RAW264.7 (sh-FAF1) cells were infected with PR8-GFP (MOI = 2). At the indicated time points after infection, β-actin were measured in cell extracts by immunoblotting to confirm equal loading of proteins. (PPTX) Click here for additional data file.

Raw data for Fig 5B.

Control RAW264.7 (Control) and FAF1-overexpressing RAW264.7 (FAF1) cells were infected with PR8-GFP (MOI = 2). At the indicated time points after infection, phosphorylated TBK1 was measured in cell extracts by immunoblotting. (PPTX) Click here for additional data file.
  1 in total

1.  FAS-associated factor-1 positively regulates type I interferon response to RNA virus infection by targeting NLRX1.

Authors:  Jae-Hoon Kim; Min-Eun Park; Chamilani Nikapitiya; Tae-Hwan Kim; Md Bashir Uddin; Hyun-Cheol Lee; Eunhee Kim; Jin Yeul Ma; Jae U Jung; Chul-Joong Kim; Jong-Soo Lee
Journal:  PLoS Pathog       Date:  2017-05-22       Impact factor: 6.823

  1 in total
  1 in total

1.  Negative regulation of NEMO signaling by the ubiquitin E3 ligase MARCH2.

Authors:  Kiramage Chathuranga; Tae-Hwan Kim; Hyuncheol Lee; Jun-Seol Park; Jae-Hoon Kim; Wijesinghe A Gayan Chathuranga; Pathum Ekanayaka; Youn Jung Choi; Chul-Ho Lee; Chul-Joong Kim; Jae U Jung; Jong-Soo Lee
Journal:  EMBO J       Date:  2020-09-16       Impact factor: 11.598

  1 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.