Filamin B Serves as a Molecular Scaffold for Type I Interferon-induced c-Jun NH2-terminal Kinase Signaling Pathway
- Authors
- Jeon, Young Joo; Choi, Joon Seok; Lee, Jung Yun; Yu, Kyung Ryun; Ka, Seung Hyeun; Cho, Yongcheol; Choi, Eui-Ju; Baek, Sung Hee; Seol, Jae Hong; Park, Dongeun; Bang, Ok Sun; Chung, Chin Ha
- Issue Date
- 12월-2008
- Publisher
- AMER SOC CELL BIOLOGY
- Citation
- MOLECULAR BIOLOGY OF THE CELL, v.19, no.12, pp.5116 - 5130
- Indexed
- SCIE
SCOPUS
- Journal Title
- MOLECULAR BIOLOGY OF THE CELL
- Volume
- 19
- Number
- 12
- Start Page
- 5116
- End Page
- 5130
- URI
- https://scholar.korea.ac.kr/handle/2021.sw.korea/122331
- DOI
- 10.1091/mbc.E08-06-0576
- ISSN
- 1059-1524
- Abstract
- Type I interferons (IFNs) activate Janus tyrosine kinase-signal transducer and activator of transcription pathway for exerting pleiotropic biological effects, including antiviral, antiproliferative, and immunomodulatory responses. Here, we demonstrate that filamin B functions as a scaffold that links between activated Rac1 and a c-Jun NH2-terminal kinase (JNK) cascade module for mediating type I IFN signaling. Filamin B interacted with Rac1, mitogen-activated protein kinase kinase kinase 1, mitogen-activated protein kinase kinase 4, and JNK. Filamin B markedly enhanced IFN alpha-dependent Rac1 activation and the sequential activation of the JNK cascade members. Complementation assays using M2 melanoma cells revealed that filamin B, but not filamin A, is required for IFN alpha-dependent activation of JNK. Furthermore, filamin B promoted IFN alpha-induced apoptosis, whereas short hairpin RNA-mediated knockdown of filamin B prevented it. These results establish a novel function of filamin B as a molecular scaffold in the JNK signaling pathway for type I IFN-induced apoptosis, thus providing the biological basis for antitumor and antiviral functions of type I IFNs.
- Files in This Item
- There are no files associated with this item.
- Appears in
Collections - Graduate School > Department of Life Sciences > 1. Journal Articles
Items in ScholarWorks are protected by copyright, with all rights reserved, unless otherwise indicated.