| Literature DB >> 16129434 |
Michael G Paine1, J Ramesh Babu, M Lamar Seibenhener, Marie W Wooten.
Abstract
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.Entities:
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Year: 2005 PMID： 16129434 DOI： 10.1016/j.febslet.2005.08.010
Source DB: PubMed Journal: FEBS Lett ISSN： 0014-5793 Impact factor: 4.124