{"69073":{"#nid":"69073","#data":{"type":"news","title":"Unstable Protein Can Mediate Effects of Cellular Stress on Prions","body":[{"value":"\u003Cp\u003EIt\u2019s a\nchicken and egg question. Where do the infectious protein particles called\nprions come from? Essentially clumps of misfolded proteins, prions cause\nneurodegenerative disorders, such as mad cow\/Creutzfeldt-Jakob disease, in\nhumans and animals. Research in fungi has suggested that sometimes prions can also\nhelp cells adapt to different conditions. Prions trigger the misfolding and\naggregation of their properly folded protein counterparts, but they usually\nneed some kind of \u201cseed\u201d to get started.\u003C\/p\u003E\n\n\u003Cp\u003EScientists\nhave studied a yeast protein called Lsb2 that can promote spontaneous prion\nformation. This unstable, short-lived protein is strongly induced by cellular\nstresses such as heat. Lsb2\u2019s properties also illustrate how cells have\ndeveloped ways to control and regulate prion formation. The results are\npublished in the July 22 issue of the journal\u0026nbsp;\u003Cem\u003EMolecular Cell\u003C\/em\u003E.\u003C\/p\u003E\n\n\u003Cp\u003EThe\nstudy was conducted by members of the Center for Nanobiology of the Macromolecular\nAssembly Disorders (NanoMAD) which is made up of scientists from the Georgia\nInstitute of Technology and Emory University. Scientists from the National\nInstitues of Health and the University of Illinois at Chicago also contributed\nto the study. The first author is senior associate Tatiana Chernova, PhD at\nEmory.\u003C\/p\u003E\n\n\u003Cp\u003EThe\naggregated, or amyloid, forms of proteins connected with several other\nneurodegenerative diseases such as Alzheimer\u2019s, Parkinson\u2019s and Huntington\u2019s\ncan, in some circumstances, act like prions. So the findings provide insight\ninto how the ways that cells deal with stress might lead to poisonous protein\naggregation in human diseases.\u003C\/p\u003E\n\n\u003Cp\u003E\u201cA\ndirect human homolog of Lsb2 doesn\u2019t exist, but there may be a protein that\nperforms the same function,\u201d said Keith Wilkinson, professor of biochemistry at\nEmory University School of Medicine. \u201cThe mechanism may say more about other\ntypes of protein aggregates than about classical prions in humans. This\nmechanism of seeding and growth may be more important for aggregate formation\nin diseases such as Huntington\u2019s.\u201d\u003C\/p\u003E\n\n\u003Cp\u003ELsb2\ndoes not appear to form stable prions by itself. Rather, it seems to bind to\nand encourage the aggregation of another protein, Sup35, which does form\nprions.\u003C\/p\u003E\n\n\u003Cp\u003E\u201cOur\nmodel is that stress induces high levels of Lsb2, which allows the accumulation\nof misfolded prion proteins,\u201d Wilkinson said. \u201cLsb2 protects enough of these\nnewborn prion particles from the quality control machinery for a few of them to\nget out.\u201d\u003C\/p\u003E\n\n\u003Cp\u003EIn\ncontinuation of previous research by Yury Chernoff, director of NanoMAD and\nprofessor in the School of Biology at Georgia Tech, the new data also show that\nin addition to promoting new prions, Lsb2 strengthens existing prions during\nstress.\u003C\/p\u003E\n\n\u003Cp\u003E\u0022Little\nis known about physiological and environmental conditions influencing amyloid\ndiseases in humans,\u0022 said Chernoff. \u0022Therefore, prophylactic\nmeasures, which could end up being more effective than therapies, are\nessentially non-existant. We hope that yeast model will help to fill this\ngap.\u0022\u003C\/p\u003E\n\n\u003Cp\u003EThe\nresearch was supported by the National Institutes of Health.\u003C\/p\u003E\u003Cp\u003E\u003Cstrong\u003EWritten\nby: 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\u003EScientists discover how an unstable protein, known as Lsb2 can control and regulate the formation of infectious protein particles called prions.\u0026nbsp;\u003C\/p\u003E","format":"limited_html"}],"field_summary_sentence":[{"value":"Scientists at Georgia Tech and Emory find protein can add strength to prions."}],"uid":"27310","created_gmt":"2011-07-29 10:13:39","changed_gmt":"2016-10-08 03:09:52","author":"David Terraso","boilerplate_text":"","field_publication":"","field_article_url":"","dateline":{"date":"2011-07-29T00:00:00-04:00","iso_date":"2011-07-29T00:00:00-04:00","tz":"America\/New_York"},"extras":[],"hg_media":{"69075":{"id":"69075","type":"image","title":"Professor Yury Chernoff","body":null,"created":"1449177228","gmt_created":"2015-12-03 21:13:48","changed":"1475894604","gmt_changed":"2016-10-08 02:43:24","alt":"Professor Yury Chernoff","file":{"fid":"193375","name":"0625150-p13-9.jpg","image_path":"\/sites\/default\/files\/images\/0625150-p13-9_0.jpg","image_full_path":"http:\/\/hg.gatech.edu\/\/sites\/default\/files\/images\/0625150-p13-9_0.jpg","mime":"image\/jpeg","size":2285975,"path_740":"http:\/\/hg.gatech.edu\/sites\/default\/files\/styles\/740xx_scale\/public\/images\/0625150-p13-9_0.jpg?itok=-rHm1pKu"}},"69070":{"id":"69070","type":"image","title":"Lsb2 Expression in Yeast Cells","body":null,"created":"1449177228","gmt_created":"2015-12-03 21:13:48","changed":"1475894604","gmt_changed":"2016-10-08 02:43:24","alt":"Lsb2 Expression in Yeast Cells","file":{"fid":"193374","name":"lsb2.jpg","image_path":"\/sites\/default\/files\/images\/lsb2_0.jpg","image_full_path":"http:\/\/hg.gatech.edu\/\/sites\/default\/files\/images\/lsb2_0.jpg","mime":"image\/jpeg","size":34413,"path_740":"http:\/\/hg.gatech.edu\/sites\/default\/files\/styles\/740xx_scale\/public\/images\/lsb2_0.jpg?itok=FmsRz_Bt"}}},"media_ids":["69075","69070"],"related_links":[{"url":"http:\/\/www.nanomad.gatech.edu\/","title":"Center for Nanobiology of the Macromolecular Assembly Disorders"},{"url":"http:\/\/www.biology.gatech.edu\/people\/yury-chernoff\/?id=yury-chernoff","title":"Yury Chernoff"}],"groups":[{"id":"1183","name":"Home"}],"categories":[{"id":"146","name":"Life Sciences and Biology"},{"id":"135","name":"Research"}],"keywords":[{"id":"4833","name":"chicago"},{"id":"4896","name":"College of Sciences"},{"id":"247","name":"Emory"},{"id":"2286","name":"nano"},{"id":"13830","name":"NanoMaD"},{"id":"2076","name":"NIH"},{"id":"13831","name":"prion"},{"id":"13827","name":"Yury Chernoff"}],"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\u003C\/p\u003E\u003Cp\u003EGeorgia Tech College of Sciences\u003C\/p\u003E\u003Cp\u003E404-385-1393\u003C\/p\u003E","format":"limited_html"}],"email":["david.terraso@cos.gatech.edu"],"slides":[],"orientation":[],"userdata":""}}}