TY - JOUR
T1 - CC2D1A, a DM14 and C2 domain protein, activates NF-κB through the canonical pathway
AU - Zhao, Meng
AU - Li, Xiao Dong
AU - Chen, Zhijian
PY - 2010/8/6
Y1 - 2010/8/6
N2 - 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 CC2D1Ais a potent activator of NF-κB. The activation of NF-κB by CC2D1A requires its C2 domain. CC2D1A activates NF-κB in a manner that depends on the ubiquitin-conjugating enzyme Ubc13, TNF receptor-associated factor TRAF2, the protein kinase TAK1, and the IκB kinase (IKK) complex. In addition, the deubiquitination enzyme Cylindromatosis (CYLD) negatively regulates the activity of CC2D1A. These results suggest that CC2D1A activates NF-κB through the canonical IKK pathway.
AB - 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 CC2D1Ais a potent activator of NF-κB. The activation of NF-κB by CC2D1A requires its C2 domain. CC2D1A activates NF-κB in a manner that depends on the ubiquitin-conjugating enzyme Ubc13, TNF receptor-associated factor TRAF2, the protein kinase TAK1, and the IκB kinase (IKK) complex. In addition, the deubiquitination enzyme Cylindromatosis (CYLD) negatively regulates the activity of CC2D1A. These results suggest that CC2D1A activates NF-κB through the canonical IKK pathway.
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U2 - 10.1074/jbc.M109.100057
DO - 10.1074/jbc.M109.100057
M3 - Article
C2 - 20529849
AN - SCOPUS:77955287060
SN - 0021-9258
VL - 285
SP - 24372
EP - 24380
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 32
ER -