Please use this identifier to cite or link to this item: http://hdl.handle.net/11455/40328
標題: Tumor Suppressor HLJ1 Binds and Functionally Alters Nucleophosmin via Activating Enhancer Binding Protein 2 alpha Complex Formation
作者: Chang, T.P.
陳健尉
Yu, S.L.
Lin, S.Y.
Hsiao, Y.J.
Chang, G.C.
Yang, P.C.
Chen, J.J.W.
關鍵字: nucleolar phosphoprotein b23;heat-shock-protein;cell lung-cancer;transcription factors;ovarian-cancer;breast-cancer;up-regulation;invasion;apoptosis;growth
Project: Cancer Research
期刊/報告no:: Cancer Research, Volume 70, Issue 4, Page(s) 1656-1667.
摘要: 
HLJ1, a member of the heat shock protein 40 chaperone family, is a newly identified tumor suppressor that has been implicated in tumorigenesis and metastasis in non-small cell lung cancer. However, the mechanism of HLJ1 action is presently obscure. In this study, we report that HLJ1 specifically interacts with the nuclear protein nucleophosmin (NPM1), forming a multiprotein complex that alters the nucleolar distribution and oligomerization state of NPM1. Enforced accumulation of NPM1 oligomers by overexpression in weakly invasive but high HLJ1-expressing cells induced the activity of signal transducer and activator of transcription 3 (STAT3) and increased cellular migration, invasiveness, and colony formation. Furthermore, silencing HLJ1 accelerated NPM1 oligomerization, inhibited the activity of transcription corepressor activating enhancer binding protein 2 alpha (AP-2 alpha), and increased the activities of matrix metalloproteinase-2 (MMP-2) and STAT3. Our findings suggest that HLJ1 switches the role of NPM1, which can act as tumor suppressor or oncogene, by modulating the oligomerization of NPM1 via HLJ1-NPM1 heterodimer formation and recruiting AP-2 alpha to the MMP-2 promoter. Cancer Res; 70(4); 1656-67. (C) 2010 AACR.
URI: http://hdl.handle.net/11455/40328
ISSN: 0008-5472
DOI: 10.1158/0008-5472.can-09-2453
Appears in Collections:生物醫學研究所

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