Fe65 does not stabilize AICD during activation of transcription in a luciferase assay

被引：12

作者：

Huysseune, Sandra ^{[1
]}

Kienlen-Campard, Pascal ^{[1
]}

Octave, Jean-Noel ^{[1
]}

机构：

[1] Univ Catholique Louvain, Ctr Neurosci, Pharmacol Lab, FARL 5410, B-1200 Brussels, Belgium

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2007年 / 361卷 / 02期

关键词：

amyloid precursor protein; AICD; Fe65; transcription; luciferase;

D O I：

10.1016/j.bbrc.2007.06.186

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 [生物化学与分子生物学]; 081704 [应用化学];

摘要：

The APP intracellular domain (AICD) could be involved in signaling via interaction with the adaptor protein Fe65, and with the histone acetyl transferase Tip60. However, the real function of AICD and Fe65 in regulation of transcription remains controversial. In this study, the human APPGa14 fusion protein was expressed in CHO cells and the transcriptional activity of AICDGa14 was measured in a luciferase-based reporter assay. AICDGaI4 was stabilized by expression of Fe65 and levels of AICDGa14 controlled luciferase activity. On the contrary, when human APP was expressed in CHO cells, coexpression of Fe65 increased luciferase activity without affecting the amount of AICD fragment. AICD produced from APP was protected from degradation by orthophenanthroline, but not by lactacystine, indicating that AICD is not a substrate of the chymotryptic activity of the proteasome. It is concluded that Fe65 can control luciferase activity without stabilizing the labile AICD fragment. (c) 2007 Elsevier Inc. All rights reserved.

引用

页码：317 / 322

页数：6

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