Please use this identifier to cite or link to this item: http://hdl.handle.net/11455/60428
標題: Phosphorylation of ARD1 by IKK beta contributes to its destabilization and degradation
作者: Kuo, H.P.
賴建成
Lee, D.F.
Xia, W.Y.
Lai, C.C.
Li, L.Y.
Hung, M.C.
關鍵字: Phosphorylation
Arrest-defective protein 1
I kappa B kinase beta
Destabilization
Degradation
nf-kappa-b
acetyltransferase complex
protein
acetylation
hif-1-alpha
hard1
yeast
gene
identification
suppression
期刊/報告no:: Biochemical and Biophysical Research Communications, Volume 389, Issue 1, Page(s) 156-161.
摘要: I kappa B kinase beta (IKK beta), a major kinase downstream of various proinflammatory signals, mediates multiple cellular functions through phosphorylation and regulation of its substrates. On the basis of protein sequence analysis, we identified arrest-defective protein 1 (ARD1), a protein involved in apoptosis and cell proliferation processes in many human cancer cells, as a new IKK beta substrate. We provided evidence showing that ARD1 is indeed a bona. de substrate of IKK beta. IKK beta physically associated with ARD1 and phosphorylated it at Ser209. Phosphorylation by IKK beta destabilized ARD1 and induced its proteasome-mediated degradation. Impaired growth suppression was observed in ARD1 phosphorylation-mimic mutant (S209E)-transfected cells as compared with ARD1 non-phosphorylatable mutant (S209A)-transfected cells. Our findings of molecular interactions between ARD1 and IKK beta may enable further understanding of the upstream regulation mechanisms of ARD1 and of the diverse functions of IKK beta. (C) 2009 Elsevier Inc. All rights reserved.
URI: http://hdl.handle.net/11455/60428
ISSN: 0006-291X
文章連結: http://dx.doi.org/10.1016/j.bbrc.2009.08.127
Appears in Collections:分子生物學研究所

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