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KMID : 0578320080260020175
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Molecules and Cells
2008 Volume.26 No. 2 p.175 ~ p.180
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A Splice Variant of the C2H2-Type Zinc Finger Protein, ZNF268s, Regulates NF-kappaB Activation by TNF-alpha
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Chun Jung-Nyeo
Lee Kong-Joo
Kang Sang-Won
Song In-Sung
Kang Dong-Hoon
Song Hye-Jin
Kim Hye-In
Suh Ja-Won
Kim Jae-Sang
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Abstract
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I?B kinase (IKK), the pivotal kinase in signal-dependent activation of nuclear factor-?B (NF-?B), is composed of multiple protein components, including IKK ?/?/? 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-?-induced NF-?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-?-induced NF-?B activation by interacting with the IKK complex.
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KEYWORD
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C2H2-type zinc finger protein, IκB kinase, KRAB, NF-κB, TNF-α, ZNF268
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