{"99961":{"#nid":"99961","#data":{"type":"news","title":"Unstable Protein Can Mediate Effects of Cellular Stress on Prions","body":[{"value":"\u003Cp\u003EIt\u0027s a chicken and egg question. Where do the infectious protein particles called prions come from? Essentially clumps of misfolded proteins, prions cause neurodegenerative disorders, such as mad cow\/Creutzfeldt-Jakob disease, in humans and animals. Research in fungi has suggested that sometimes prions can also help cells adapt to different conditions. Prions trigger the misfolding and aggregation of their properly folded protein counterparts, but they usually need some kind of \u0022seed\u0022 to get started.\u003C\/p\u003E\u003Cp\u003EScientists have studied a yeast protein called Lsb2 that can promote spontaneous prion formation. This unstable, short-lived protein is strongly induced by cellular stresses such as heat. Lsb2\u0027s properties also illustrate how cells have developed ways to control and regulate prion formation. The results are published in the July 22 issue of the journal \u003Cem\u003EMolecular Cell\u003C\/em\u003E.\u003C\/p\u003E\u003Cp\u003EThe study was conducted by members of the Center for Nanobiology of the Macromolecular Assembly Disorders (NanoMAD) which is made up of scientists from the Georgia Institute of Technology and Emory University. Scientists from the National Institues of Health and the University of Illinois at Chicago also contributed to the study. The first author is senior associate Tatiana Chernova, PhD at Emory.\u003C\/p\u003E\u003Cp\u003EThe aggregated, or amyloid, forms of proteins connected with several other neurodegenerative diseases such as Alzheimer\u0027s, Parkinson\u0027s and Huntington\u00e2\u0080\u0099s can, in some circumstances, act like prions. So the findings provide insight into how the ways that cells deal with stress might lead to poisonous protein aggregation in human diseases.\u003C\/p\u003E\u003Cp\u003E\u0022A direct human homolog of Lsb2 doesn\u00e2\u0080\u0099t exist, but there may be a protein that performs the same function,\u0022 said Keith Wilkinson, professor of biochemistry at Emory University School of Medicine. \u0022The mechanism may say more about other types of protein aggregates than about classical prions in humans. This mechanism of seeding and growth may be more important for aggregate formation in diseases such as Huntington\u0027s.\u0022\u003C\/p\u003E\u003Cp\u003ELsb2 does not appear to form stable prions by itself. Rather, it seems to bind to and encourage the aggregation of another protein, Sup35, which does form prions.\u003C\/p\u003E\u003Cp\u003E\u0022Our model is that stress induces high levels of Lsb2, which allows the accumulation of misfolded prion proteins,\u0022 Wilkinson said. \u0022Lsb2 protects enough of these newborn prion particles from the quality control machinery for a few of them to get out.\u0022\u003C\/p\u003E\u003Cp\u003EIn continuation of previous research by Yury Chernoff, director of NanoMAD and professor in the School of Biology at Georgia Tech, the new data also show that in addition to promoting new prions, Lsb2 strengthens existing prions during stress.\u003C\/p\u003E\u003Cp\u003E\u0022Little is known about physiological and environmental conditions influencing amyloid diseases in humans,\u0022 said Chernoff. \u0022Therefore, prophylactic measures, which could end up being more effective than therapies, are essentially non-existant. We hope that yeast model will help to fill this gap.\u0022\u003C\/p\u003E\u003Cp\u003EThe research was supported by the National Institutes of Health.\u003C\/p\u003E\u003Cp\u003E\u003Cstrong\u003EWritten by: Emory University and the Georgia Institute of Technology\u003C\/strong\u003E\u003C\/p\u003E","summary":null,"format":"limited_html"}],"field_subtitle":"","field_summary":[{"value":"\u003Cp\u003EIt\u0027s a chicken and egg question. Where do the infectious protein particles called prions come from? Essentially clumps of misfolded proteins, prions cause neurodegenerative disorders, such as mad cow\/Creutzfeldt-Jakob disease, in humans and animals.\u003C\/p\u003E","format":"limited_html"}],"field_summary_sentence":[{"value":"Unstable Protein Can Mediate Effects of Cellular Stress on Prions"}],"uid":"27245","created_gmt":"2011-08-08 00:00:00","changed_gmt":"2022-05-26 17:09:36","author":"Troy Hilley","boilerplate_text":"","field_publication":"","field_article_url":"","dateline":{"date":"2011-08-08T00:00:00-04:00","iso_date":"2011-08-08T00:00:00-04:00","tz":"America\/New_York"},"extras":[],"hg_media":{"99971":{"id":"99971","type":"image","title":"Lsb2 Expression in Yeast Cells","body":null,"created":"1449178150","gmt_created":"2015-12-03 21:29:10","changed":"1475894715","gmt_changed":"2016-10-08 02:45:15"}},"media_ids":["99971"],"related_links":[{"url":"http:\/\/www.biology.gatech.edu\/people\/yury-chernoff","title":"Yury Chernoff"},{"url":"http:\/\/www.nanomad.gatech.edu\/","title":"Center for Nanobiology of the Macromolecular Assembly Disorders"},{"url":"http:\/\/www.biology.gatech.edu\/","title":"School of Biology"}],"groups":[{"id":"1275","name":"School of Biological Sciences"}],"categories":[{"id":"146","name":"Life Sciences and Biology"}],"keywords":[],"core_research_areas":[],"news_room_topics":[],"event_categories":[],"invited_audience":[],"affiliations":[],"classification":[],"areas_of_expertise":[],"news_and_recent_appearances":[],"phone":[],"contact":[{"value":"\u003Cp\u003EDavid Terraso - Georgia Tech College of Sciences\u003C\/p\u003E","format":"limited_html"}],"email":["david.terraso@cos.gatech.edu"],"slides":[],"orientation":[],"userdata":""}}}