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J Biol Chem. 2010 Aug 6;285(32):24372-80. doi: 10.1074/jbc.M109.100057. Epub 2010 Jun 7.

CC2D1A, a DM14 and C2 domain protein, activates NF-kappaB through the canonical pathway.

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  • 1Department of Molecular Biology, University of Texas Southwestern Medical Center at Dallas, Dallas, Texas 75390-9148, USA.


CC2D1A is an evolutionarily conserved protein that contains four DM14 domains at the N terminus and a C2 domain at the C terminus. Loss-of-function mutations in CC2D1A have been linked to mental retardation in human, but the biochemical function of this protein is largely unknown. Here, we show that CC2D1A is a potent activator of NF-kappaB. The activation of NF-kappaB by CC2D1A requires its C2 domain. CC2D1A activates NF-kappaB in a manner that depends on the ubiquitin-conjugating enzyme Ubc13, TNF receptor-associated factor TRAF2, the protein kinase TAK1, and the IkappaB kinase (IKK) complex. In addition, the deubiquitination enzyme Cylindromatosis (CYLD) negatively regulates the activity of CC2D1A. These results suggest that CC2D1A activates NF-kappaB through the canonical IKK pathway.

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