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The polyproteins are further cleaved by 3C\u2010like cysteine protease (3CL\n                    <jats:sup>pro<\/jats:sup>\n                    ) and papain\u2010like protease (PL\n                    <jats:sup>pro<\/jats:sup>\n                    ) into 16 nonstructural proteins (nsps). PL\n                    <jats:sup>pro<\/jats:sup>\n                    is released from nsp3 through autocleavage, and then it cleaves the sites between nsp1\/2, between nsp2\/3 and between nsp3\/4 with recognition motif of LXGG, and the sites in the C\u2010terminus of ubiquitin and of protein interferon\u2010stimulated gene 15 (ISG15) with recognition motif of RLRGG. Alone or together with SARS unique domain (SUD), PL\n                    <jats:sup>pro<\/jats:sup>\n                    can stabilize an E3 ubiquitin ligase, the ring\u2010finger, and CHY zinc\u2010finger domain\u2010containing 1 (RCHY1), through domain interaction, and thus, promote RCHY1 to ubiquitinate its target proteins including p53. However, a dilemma appears in terms of PL\n                    <jats:sup>pro<\/jats:sup>\n                    roles. On the one hand, the ubiquitination of p53 is good for SARS\u2010CoV because the ubiquitinated p53 cannot inhibit SARS\u2010CoV replication. On the other hand, the ubiquitination of NF\u2010\u03baB inhibitor (I\u03baB\u03b1), TNF receptor\u2010associated factors (TRAFs), and stimulator of interferon gene (STING), and the ISGylation of targeted proteins are bad for SARS\u2010CoV because these ubiquitination and ISGylation initiate the innate immune response and antiviral state. This mini\u2010review analyzes the dilemma and provides a snapshot on how the viral PL\n                    <jats:sup>pro<\/jats:sup>\n                    smartly manages its roles to avoid its simultaneously contradictory actions, which could shed lights on possible strategies to deal with SARS\u2010CoV\u20102 infections.\n                  <\/jats:p>","DOI":"10.1096\/fj.202002271","type":"journal-article","created":{"date-parts":[[2020,12,28]],"date-time":"2020-12-28T07:29:12Z","timestamp":1609140552000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":36,"title":["Spatial and temporal roles of SARS\u2010CoV PL\n                    <sup>pro<\/sup>\n                    \u2014A snapshot"],"prefix":"10.1096","volume":"35","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-7642-3972","authenticated-orcid":false,"given":"Shaomin","family":"Yan","sequence":"first","affiliation":[{"name":"National Engineering Research Center for Non\u2010Food Biorefinery State Key Laboratory of Non\u2010Food Biomass and Enzyme Technology Guangxi Biomass Engineering Technology Research Center Guangxi Key Laboratory of Bio\u2010Refinery Guangxi Academy of Sciences Nanning China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-0775-5759","authenticated-orcid":false,"given":"Guang","family":"Wu","sequence":"additional","affiliation":[{"name":"National Engineering Research Center for Non\u2010Food Biorefinery State Key Laboratory of Non\u2010Food Biomass and Enzyme Technology Guangxi Biomass Engineering Technology Research Center Guangxi Key Laboratory of Bio\u2010Refinery Guangxi Academy of Sciences Nanning China"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2020,12,28]]},"reference":[{"key":"e_1_2_8_2_1","doi-asserted-by":"publisher","DOI":"10.1007\/3-540-26765-4_1"},{"key":"e_1_2_8_3_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0022-2836(03)00865-9"},{"key":"e_1_2_8_4_1","doi-asserted-by":"publisher","DOI":"10.1099\/vir.0.19424-0"},{"key":"e_1_2_8_5_1","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.1601327113"},{"key":"e_1_2_8_6_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.antiviral.2014.12.015"},{"key":"e_1_2_8_7_1","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M104097200"},{"key":"e_1_2_8_8_1","first-page":"1","article-title":"Comparative analysis of amino acid sequences of key enzymes of replication and expression of positive\u2010strand RNA viruses. 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