{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,25]],"date-time":"2026-08-25T16:01:48Z","timestamp":1787673708141,"version":"build-2736575974"},"reference-count":55,"publisher":"The Company of Biologists","issue":"7","license":[{"start":{"date-parts":[[2021,4,1]],"date-time":"2021-04-01T00:00:00Z","timestamp":1617235200000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/www.biologists.com\/user-licence-1-1\/"}],"funder":[{"DOI":"10.13039\/100000048","name":"American Cancer Society","doi-asserted-by":"crossref","award":["RSG-19-022-01-CSM"],"award-info":[{"award-number":["RSG-19-022-01-CSM"]}],"id":[{"id":"10.13039\/100000048","id-type":"DOI","asserted-by":"crossref"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"crossref","award":["R01-GM127557"],"award-info":[{"award-number":["R01-GM127557"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"crossref"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"crossref","award":["2R25GM066567"],"award-info":[{"award-number":["2R25GM066567"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"crossref"}]},{"DOI":"10.13039\/100008090","name":"Tufts University","doi-asserted-by":"crossref","id":[{"id":"10.13039\/100008090","id-type":"DOI","asserted-by":"crossref"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2021,4,1]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n                  <jats:p>The recognition and disposal of misfolded proteins is essential for the maintenance of cellular homeostasis. Perturbations in the pathways that promote degradation of aberrant proteins contribute to a variety of protein aggregation disorders broadly termed proteinopathies. The AAA-ATPase p97 (also known as VCP), in combination with adaptor proteins, functions to identify ubiquitylated proteins and target them for degradation by the proteasome or through autophagy. Mutations in p97 cause multi-system proteinopathies; however, the precise defects underlying these disorders are unclear. Here, we systematically investigate the role of p97 and its adaptors in the process of formation of aggresomes, membrane-less structures containing ubiquitylated proteins that arise upon proteasome inhibition. We demonstrate that p97 mediates aggresome formation and clearance, and identify a novel role for the adaptor UBXN1 in the process of aggresome formation. UBXN1 is recruited to aggresomes, and UBXN1-knockout cells are unable to form aggresomes. Loss of p97\u2013UBXN1 results in increased Huntingtin polyQ inclusion bodies both in mammalian cells and in a C. elegans model of Huntington's disease. Together, our results identify evolutionarily conserved roles for p97\u2013UBXN1 in the disposal of protein aggregates.<\/jats:p>","DOI":"10.1242\/jcs.254201","type":"journal-article","created":{"date-parts":[[2021,3,12]],"date-time":"2021-03-12T06:55:16Z","timestamp":1615532116000},"source":"Crossref","is-referenced-by-count":30,"title":["The p97\u2013UBXN1 complex regulates aggresome formation"],"prefix":"10.1242","volume":"134","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-8875-7985","authenticated-orcid":false,"given":"Sirisha","family":"Mukkavalli","sequence":"first","affiliation":[{"name":"Tufts University School of Medicine 1 Department of Developmental Molecular and Chemical Biology , , Boston, MA 02111 , USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-0759-4724","authenticated-orcid":false,"given":"Jacob Aaron","family":"Klickstein","sequence":"additional","affiliation":[{"name":"Tufts University School of Medicine 1 Department of Developmental Molecular and Chemical Biology , , Boston, MA 02111 , USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Betty","family":"Ortiz","sequence":"additional","affiliation":[{"name":"Tufts University School of Medicine 2 Department of Developmental Molecular and Chemical Biology , , Boston, MA 02111 , USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-3039-2266","authenticated-orcid":false,"given":"Peter","family":"Juo","sequence":"additional","affiliation":[{"name":"Tufts University School of Medicine 2 Department of Developmental Molecular and Chemical Biology , , Boston, MA 02111 , USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-4773-8673","authenticated-orcid":false,"given":"Malavika","family":"Raman","sequence":"additional","affiliation":[{"name":"Tufts University School of Medicine 1 Department of Developmental Molecular and Chemical Biology , , Boston, MA 02111 , USA"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"237","published-online":{"date-parts":[[2021,4,15]]},"reference":[{"key":"2024061307434433200_JCS254201C1","doi-asserted-by":"publisher","first-page":"805","DOI":"10.1038\/nature02998","article-title":"Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death","volume":"431","author":"Arrasate","year":"2004","journal-title":"Nature"},{"key":"2024061307434433200_JCS254201C2","doi-asserted-by":"publisher","first-page":"179","DOI":"10.1016\/j.cell.2017.08.009","article-title":"In Situ architecture and cellular interactions of PolyQ inclusions","volume":"171","author":"Bauerlein","year":"2017","journal-title":"Cell"},{"key":"2024061307434433200_JCS254201C3","doi-asserted-by":"publisher","first-page":"229","DOI":"10.1083\/jcb.201511024","article-title":"Protein misfolding specifies recruitment to cytoplasmic inclusion bodies","volume":"213","author":"Bersuker","year":"2016","journal-title":"J Cell Biol."},{"key":"2024061307434433200_JCS254201C4","doi-asserted-by":"publisher","first-page":"E4380","DOI":"10.1073\/pnas.1706205114","article-title":"Ubiquitin- and ATP-dependent unfoldase activity of P97\/VCP*NPLOC4*UFD1L is enhanced by a mutation that causes multisystem proteinopathy","volume":"114","author":"Blythe","year":"2017","journal-title":"Proc. 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