{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,15]],"date-time":"2026-05-15T22:35:34Z","timestamp":1778884534653,"version":"3.51.4"},"reference-count":72,"publisher":"American Society for Microbiology","issue":"1","license":[{"start":{"date-parts":[[2012,1,1]],"date-time":"2012-01-01T00:00:00Z","timestamp":1325376000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["Eukaryot Cell"],"published-print":{"date-parts":[[2012,1]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            SCF (Skp1\u2013cullin\/Cdc53\u2013F-box protein) ubiquitin ligases bind substrates via the variable F-box protein and, in conjunction with the RING domain protein Rbx1 and the ubiquitin-conjugating enzyme Ubc3\/Cdc34, catalyze substrate ubiquitination. The cullin subunit can be modified covalently by conjugation of the ubiquitin-like protein Rub1\/NEDD8 (neddylation) or bound noncovalently by the protein CAND1 (cullin-associated, neddylation-dissociated). Expression of the\n            <jats:named-content content-type=\"genus-species\">Candida albicans<\/jats:named-content>\n            CAND1 gene homolog Ca\n            <jats:italic>TIP120<\/jats:italic>\n            in\n            <jats:named-content content-type=\"genus-species\">Saccharomyces cerevisiae<\/jats:named-content>\n            is toxic only in the presence of CaCdc53, consistent with a specific interaction between CaTip120 and CaCdc53. To genetically analyze this system in\n            <jats:named-content content-type=\"genus-species\">C. albicans<\/jats:named-content>\n            , we deleted the homologs of\n            <jats:italic>RUB1<\/jats:italic>\n            \/NEDD8,\n            <jats:italic>TIP120<\/jats:italic>\n            \/CAND1, and the deneddylase gene\n            <jats:italic>JAB1<\/jats:italic>\n            , and we also generated a temperature-sensitive allele of the essential Ca\n            <jats:italic>CDC53<\/jats:italic>\n            gene by knock-in site-directed mutagenesis. Deletion of Ca\n            <jats:italic>RUB1<\/jats:italic>\n            and Ca\n            <jats:italic>TIP120<\/jats:italic>\n            caused morphological, growth, and protein degradation phenotypes consistent with a reduction in SCF ubiquitin ligase activity. Furthermore, the double Ca\n            <jats:italic>rub1<\/jats:italic>\n            <jats:sup>\u2212\/\u2212<\/jats:sup>\n            Ca\n            <jats:italic>tip120<\/jats:italic>\n            <jats:sup>\u2212\/\u2212<\/jats:sup>\n            mutant was more defective in SCF activity than either individual deletion mutant. These results indicate that CAND1 stimulates SCF ubiquitin ligase activity and that it does so independently of neddylation. Our data do not support a role for CAND1 in the protection of either the F-box protein or cullin from degradation but are consistent with the suggested role of CAND1 in SCF complex remodeling.\n          <\/jats:p>","DOI":"10.1128\/ec.05250-11","type":"journal-article","created":{"date-parts":[[2011,11,12]],"date-time":"2011-11-12T04:13:09Z","timestamp":1321071189000},"page":"42-52","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":13,"title":["Neddylation and CAND1 Independently Stimulate SCF Ubiquitin Ligase Activity in Candida albicans"],"prefix":"10.1128","volume":"11","author":[{"given":"Nadine","family":"Sela","sequence":"first","affiliation":[{"name":"Department of Molecular Microbiology, B. 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