Evidence for p62 aggregate formation: Role in cell survival

被引：43

作者：

Paine, MG ^{[1
]}

Babu, JR ^{[1
]}

Seibenhener, ML ^{[1
]}

Wooten, MW ^{[1
]}

机构：

[1] Auburn Univ, Program Cell & Mol Biosci, Auburn, AL 36849 USA

来源：

FEBS LETTERS | 2005年 / 579卷 / 22期

关键词：

p62; protein aggregation; Alzheimer's disease; sequestosome;

D O I：

10.1016/j.febslet.2005.08.010

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 polyubiquitin-binding protein p62 has been shown to localize in aggregates common to several types of diseases. Here, we report that p62 forms independent fibrillar aggregates in vitro in a time- and concentration-dependent manner. FTIR spectra and ThT fluorescence assay of p62 reveals increased beta-sheet content as aggregates form compared to the native protein. The fibrillar nature of the aggregates was observed by transmission electron microscopy. Overexpression of p62 in HEK cells results in aggregate formation that may protect cells from apoptosis. Altogether, these results suggest that p62 fibrils may influence cell viability and indicates an important role for p62 in aggresome formation. (c) 2005 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

引用

页码：5029 / 5034

页数：6

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