Roles of the intramolecular regions of FE65 in its trans-accumulation and in p53 stabilization in the nuclear matrix of osmotically stressed cells

被引：3

作者：

Kawai, Tomoko ^{[1
]}

Nakaya, Tadashi ^{[1
]}

Suzuki, Toshiharu ^{[1
]}

机构：

[1] Hokkaido Univ, Grad Sch Pharmaceut Sci, Lab Neurosci, Kita Ku, Sapporo, Hokkaido 0600812, Japan

来源：

FEBS LETTERS | 2010年 / 584卷 / 04期

关键词：

Phosphotyrosine interaction domain; FE65; Amyloid beta-protein precursor; Hyperosmotic stress; AMYLOID PRECURSOR PROTEIN; PHOSPHORYLATION; DOMAINS; WW;

D O I：

10.1016/j.febslet.2009.12.040

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The neural adaptor protein FE65 interacts with the amyloid beta-protein precursor (APP). In osmotically stressed cells, the membrane APP-tethered FE65 is released into the cytoplasm and translocates to the nuclear matrix, where it stabilizes p53 via a non-canonical pathway. In this study, we found that the second phosphotyrosine interaction domain (PI2) of FE65 mediated its trans-accumulation in the nuclear matrix of osmotically stressed cells. The carboxyl-terminal half of FE65, which contains the PI2 domain, failed to stabilize p53, suggesting that the amino-terminal half of the protein plays an important role in the stabilization of p53 in osmotically stressed cells. (C) 2009 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.

引用

页码：765 / 769

页数：5