{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,17]],"date-time":"2026-08-17T22:08:10Z","timestamp":1787004490358,"version":"build-2736575974"},"reference-count":42,"publisher":"Portland Press Ltd.","issue":"12","license":[{"start":{"date-parts":[[2021,6,18]],"date-time":"2021-06-18T00:00:00Z","timestamp":1623974400000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by-nc-nd\/4.0\/"}],"content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[2021,6,25]]},"abstract":"<jats:p>Autophagy is an important component of the innate immune response that restricts infection by different types of pathogens. Viruses have developed multiple strategies to avoid autophagy to complete their replication cycle and promote spreading to new hosts. Here, we report that the ubiquitin deconjugases encoded in the N-terminal domain of the large tegument proteins of Epstein\u2013Barr virus (EBV), Kaposi Sarcoma herpesvirus (KSHV) and human cytomegalovirus (HCMV), but not herpes simplex virus-1 (HSV-1), regulate selective autophagy by inhibiting the activity of the autophagy receptor SQSTM1\/p62. We found that all the homologs bind to and deubiquitinate SQSTM1\/p62 but with variable efficiency, which correlates with their capacity to prevent the colocalization of light chain 3 (LC3) with SQSTM1\/p62 aggregates and promote the accumulation of a model autophagy substrate. The findings highlight important differences in the strategies by which herpesviruses interfere with selective autophagy.<\/jats:p>","DOI":"10.1042\/bcj20210225","type":"journal-article","created":{"date-parts":[[2021,6,18]],"date-time":"2021-06-18T12:27:25Z","timestamp":1624019245000},"page":"2297-2308","update-policy":"https:\/\/doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":10,"title":["Inhibition of selective autophagy by members of the herpesvirus ubiquitin-deconjugase family"],"prefix":"10.1042","volume":"478","author":[{"given":"P\u00e4ivi","family":"Yl\u00e4-Anttila","sequence":"first","affiliation":[{"name":"Department of Cell and Molecular Biology, Karolinska Institutet, S-17165 Stockholm, Sweden"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-5541-2809","authenticated-orcid":false,"given":"Maria G.","family":"Masucci","sequence":"additional","affiliation":[{"name":"Department of Cell and Molecular Biology, Karolinska Institutet, S-17165 Stockholm, Sweden"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"288","published-online":{"date-parts":[[2021,6,18]]},"reference":[{"key":"2021112218220882200_BCJ-2021-0225C1","doi-asserted-by":"publisher","first-page":"1717","DOI":"10.1126\/science.290.5497.1717","article-title":"Autophagy as a regulated pathway of cellular degradation","volume":"290","year":"2000","journal-title":"Science"},{"key":"2021112218220882200_BCJ-2021-0225C2","doi-asserted-by":"publisher","first-page":"57","DOI":"10.1038\/cdd.2008.130","article-title":"Eating the enemy within: autophagy in infectious diseases","volume":"16","year":"2009","journal-title":"Cell Death Differ."},{"key":"2021112218220882200_BCJ-2021-0225C3","doi-asserted-by":"publisher","first-page":"421","DOI":"10.1247\/csf.27.421","article-title":"Autophagosome formation in mammalian cells","volume":"27","year":"2002","journal-title":"Cell Struct. 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