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Splice variant of the C2H2-type zinc finger protein, ZNF268s, regulates NF-kappa B activation by TNF-alpha
- Splice variant of the C2H2-type zinc finger protein, ZNF268s, regulates NF-kappa B activation by TNF-alpha
- Chun, Jung Nyeo; Song, In Sung; Kang, Dong-Hoon; Song, Hye Jin; Kim, Hye In; Suhl, Ja Won; Lee, Kong Ju; Kim, Jaesang; Kang, Sang Won
- Ewha Authors
- 이공주; 강상원; 김재상; 강동훈
- SCOPUS Author ID
- 이공주; 강상원; 김재상; 강동훈
- Issue Date
- Journal Title
- MOLECULES AND CELLS
- vol. 26, no. 2, pp. 175 - 180
- C2H2-type zinc finger protein; I kappa B kinase; KRAB; NF-kappa B; TNF-alpha; ZNF268
- KOREAN SOC MOLECULAR & CELLULAR BIOLOGY
- SCI; SCIE; SCOPUS; KCI
- I kappa B kinase (IKK), the pivotal kinase in signal-dependent activation of nuclear factor-kappa B (NF-kappa B), is composed of multiple protein components, including IKK alpha/beta/gamma core subunits. To investigate the regulation of the IKK complex, we immunoaffinity purified the IKK complex, and by MALDI-TOF mass spectrometry identified a splice variant of zinc finger protein 268 (ZNF268) as a novel IKK-interacting protein. Both the full-length and the spliced form of the ZNF268 protein were detected in a variety of mammalian tissues and cell lines. The genes were cloned and expressed by in vitro transcription/translation. Several deletion derivatives, such as KRAB domain (KRAB) on its own, the KRAB/spacer/4-zinc fingers (zF4), and the spacer/4-zinc fingers (zS4), were ectopically expressed in mammalian cells and exhibited had different subcellular locations. The KRAB-containing mutants were restricted to the nucleus, while zS4 was localized in the cytosol. TNF-alpha-induced NF-kappa B activation was examined using these mutants and only zS4 was found to stimulate activation. Collectively, the results indicate that a spliced form of ZNF268 lacking the KRAB domain is located in the cytosol, where it seems to play a role in TNF-alpha-induced NF-kappa B activation by interacting with the IKK complex.
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