Evidence for p62 aggregate formation: Role in cell survival

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...

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Bibliographic Details
Published in:FEBS letters 2005-09, Vol.579 (22), p.5029-5034
Main Authors: Paine, Michael G., Ramesh Babu, J., Seibenhener, M. Lamar, Wooten, Marie W.
Format: Article
Language:English
Subjects:
Adaptor Proteins, Signal Transducing
Alzheimer's disease
Cell Line
Cell Survival
Fourier transform infrared
FTIR
GFP
glutathione S-transferase
green fluorescent protein
GST
HEK
human embryonic kidney
Humans
Huntington's disease
Lewy body
Multiprotein Complexes - ultrastructure
NF-κB
nuclear factor κB
p62
Parkinson's disease
PB1
Phox and Bem1p
Protein aggregation
Protein Conformation
Proteins - chemistry
Proteins - genetics
Proteins - metabolism
Proteins - ultrastructure
Recombinant Fusion Proteins - chemistry
Recombinant Fusion Proteins - genetics
Recombinant Fusion Proteins - metabolism
Sequestosome
Sequestosome-1 Protein
Spectroscopy, Fourier Transform Infrared
TEM
Thioflavin T
ThT
transmission electron microscopy
UBA
ubiquitin associated
ubiquitin–proteasome system
UPS
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Summary: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 β-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.
ISSN:0014-5793
1873-3468
DOI:10.1016/j.febslet.2005.08.010