@article {310965,
	title = {Identification of MOAG-4/SERF as a regulator of age-related proteotoxicity.},
	journal = {Cell},
	volume = {142},
	year = {2010},
	month = {08/2010},
	pages = {601-12},
	abstract = {<p>Fibrillar protein aggregates are the major pathological hallmark of several incurable, age-related, neurodegenerative disorders. These aggregates typically contain aggregation-prone pathogenic proteins, such as amyloid-beta in Alzheimer{\textquoteright}s disease and alpha-synuclein in Parkinson{\textquoteright}s disease. It is, however, poorly understood how these aggregates are formed during cellular aging. Here we identify an evolutionarily highly conserved modifier of aggregation, MOAG-4, as a positive regulator of aggregate formation in C. elegans models for polyglutamine diseases. Inactivation of MOAG-4 suppresses the formation of compact polyglutamine aggregation intermediates that are required for aggregate formation. The role of MOAG-4 in driving aggregation extends to amyloid-beta and alpha-synuclein and is evolutionarily conserved in its human orthologs SERF1A and SERF2. MOAG-4/SERF appears to act independently from HSF-1-induced molecular chaperones, proteasomal degradation, and autophagy. Our results suggest that MOAG-4/SERF regulates age-related proteotoxicity through a previously unexplored pathway, which will open up new avenues for research on age-related, neurodegenerative diseases.</p>
},
	keywords = {alpha-Synuclein, Amyloid beta-Peptides, Animals, Caenorhabditis elegans, Caenorhabditis elegans Proteins, Cell Aging, Cell Line, Cell Line, Tumor, Humans, Mice, Nerve Tissue Proteins, Neurodegenerative Diseases, Peptides, Proteins},
	issn = {1097-4172},
	doi = {10.1016/j.cell.2010.07.020},
	author = {van Ham, Tjakko J and Holmberg, Mats A and van der Goot, Annemieke T and Teuling, Eva and Garcia-Arencibia, Moises and Kim, Hyun-eui and Du, Deguo and Thijssen, Karen L and Wiersma, Marit and Burggraaff, Rogier and van Bergeijk, Petra and van Rheenen, Jeroen and Jerre van Veluw, G and Hofstra, Robert M W and Rubinsztein, David C and Nollen, Ellen A A}
}
