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While much of the aggregated protein consists of disease specific proteins, such as amyloid\u2010\u03b2, \u03b1\u2010synuclein, or superoxide dismutase1 (SOD1), many other proteins are known to aggregate in these disorders. Although the role of protein aggregates in the pathogenesis of neurodegenerative diseases remains unknown, the ubiquitous association of misfolded and aggregated proteins indicates that significant dysfunction in protein homeostasis (proteostasis) occurs in these diseases. Proteostasis is the concept that the integrity of the proteome is in fine balance and requires proteins in a specific conformation, concentration, and location to be functional. In this review, we discuss the role of specific mechanisms, both inside and outside cells, which maintain proteostasis, including molecular chaperones, protein degradation pathways, and the active formation of inclusions, in neurodegenerative diseases associated with protein aggregation.<\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:label\/>\n                    <jats:p>\n                      <jats:boxed-text content-type=\"graphic\" position=\"anchor\">\n                        <jats:graphic xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" mimetype=\"image\/png\" position=\"anchor\" specific-use=\"enlarged-web-image\" xlink:href=\"graphic\/jnc13575-fig-0003-m.png\">\n                          <jats:alt-text>image<\/jats:alt-text>\n                        <\/jats:graphic>\n                      <\/jats:boxed-text>\n                      A characteristic of many neurodegenerative diseases is the aggregation of specific proteins, which alone provides strong evidence that protein homeostasis is disrupted in these disease states. Proteostasis is the maintenance of the proteome in the correct conformation, concentration, and location by functional pathways such as molecular chaperones and protein degradation machinery. Here, we discuss the potential roles of quality control pathways, both inside and outside cells, in the loss of proteostasis during aging and disease.\n                    <\/jats:p>\n                  <\/jats:sec>","DOI":"10.1111\/jnc.13575","type":"journal-article","created":{"date-parts":[[2016,2,12]],"date-time":"2016-02-12T10:55:07Z","timestamp":1455274507000},"page":"489-505","source":"Crossref","is-referenced-by-count":230,"title":["Walking the tightrope: proteostasis and neurodegenerative disease"],"prefix":"10.1111","volume":"137","author":[{"given":"Justin J.","family":"Yerbury","sequence":"first","affiliation":[{"name":"Proteostasis and Disease Research Centre School of Biological Sciences Faculty of Science, Medicine and Health University of Wollongong Wollongong New South Wales Australia"},{"name":"Illawarra Health and Medical Research Institute Wollongong New South Wales Australia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lezanne","family":"Ooi","sequence":"additional","affiliation":[{"name":"Proteostasis and Disease Research Centre School of Biological Sciences Faculty of Science, Medicine and Health University of Wollongong Wollongong New South Wales Australia"},{"name":"Illawarra Health and Medical Research Institute Wollongong New South Wales Australia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Andrew","family":"Dillin","sequence":"additional","affiliation":[{"name":"Department of Molecular and Cell Biology Li Ka Shing Center for Biomedical and Health Sciences The University of California California USA"},{"name":"Howard Hughes Medical Institute The University of California Berkeley California USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Darren N.","family":"Saunders","sequence":"additional","affiliation":[{"name":"School of Medical Sciences Faculty of Medicine University of New South Wales Randwick New South Wales Australia"},{"name":"The Kinghorn Cancer Centre Garvan Institute of Medical Research Darlinghurst New South Wales Australia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Danny M.","family":"Hatters","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Molecular Biology and Bio21 Molecular Science and Biotechnology Institute University of Melbourne Parkville Victoria Australia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Philip M.","family":"Beart","sequence":"additional","affiliation":[{"name":"Florey Institute of Neuroscience and Mental Health University of Melbourne Parkville Victoria Australia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Neil R.","family":"Cashman","sequence":"additional","affiliation":[{"name":"Department of Medicine (Neurology) University of British Columbia and Vancouver Coastal Health Research Institute Brain Research Centre University of British Columbia Vancouver British Columbia Canada"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mark R.","family":"Wilson","sequence":"additional","affiliation":[{"name":"Proteostasis and Disease Research Centre School of Biological Sciences Faculty of Science, Medicine and Health University of Wollongong Wollongong New South Wales Australia"},{"name":"Illawarra Health and Medical Research Institute Wollongong New South Wales Australia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Heath","family":"Ecroyd","sequence":"additional","affiliation":[{"name":"Proteostasis and Disease Research Centre School of Biological Sciences Faculty of Science, Medicine and Health University of Wollongong Wollongong New South Wales Australia"},{"name":"Illawarra Health and Medical Research Institute Wollongong New South Wales Australia"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2016,3,8]]},"reference":[{"issue":"13","key":"e_1_2_13_2_1","doi-asserted-by":"crossref","first-page":"2491","DOI":"10.1242\/jcs.114.13.2491","article-title":"A molecular chaperone complex at the lysosomal membrane is required for protein translocation","volume":"114","author":"Agarraberes F. 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