A splice variant of the C2H2-type zinc finger protein, ZNF268s, regulates NF-κB activation by TNF-α

Jung Nyeo Chun, In Sung Song, Dong Hoon Kang, Hye Jin Song, Hye In Kim, Ja Won Suh, Kong Ju Lee, Jaesang Kim, Sang Won Kang

Research output: Contribution to journalArticlepeer-review

7 Scopus citations


IκB kinase (IKK), the pivotal kinase in signal-dependent activation of nuclear factor-κB (NF-κB), is composed of multiple protein components, including IKK α/β/γ 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-α-induced NF-κB 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-α-induced NF-κB activation by interacting with the IKK complex.

Original languageEnglish
Pages (from-to)175-180
Number of pages6
JournalMolecules and Cells
Issue number2
StatePublished - 31 Aug 2008


  • CH-type zinc finger protein
  • IκB kinase
  • KRAB
  • NF-κB
  • TNF-α
  • ZNF268


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