{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,12]],"date-time":"2026-03-12T04:55:53Z","timestamp":1773291353672,"version":"3.50.1"},"reference-count":36,"publisher":"Portland Press Ltd.","issue":"1","content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[2010,2,1]]},"abstract":"<jats:p>The 26S proteasome is a non-lysosomal protease in the cytosol and nucleus of eukaryotic cells. Its main function is to mediate ubiquitin-dependent proteolysis. The 26S proteasome is a multimeric complex composed by the 20S proteasome CP (core particle) and the 19S RPs (regulatory particles). Although the atomic structure of the 26S proteasome has not yet been determined, high-resolution structures are available for its CP. Studies on the complicated assembly pathway of the proteasome have revealed that it involves an unprecedented number of dedicated chaperones. Assembly of the CP alone involves three conserved proteasome-assembly chaperones [PAC1\u2013PAC2, PAC3\u2013PAC4 and UMP1 (ubiquitin-mediated proteolysis 1)]. Whereas the two heterodimeric PACs have been implicated in the formation of rings of the seven distinct \u03b1 subunits, UMP1 is important for the formation and dimerization of proteasome precursor complexes containing \u03b2 subunits. Dimerization coincides with the incorporation of the last \u03b2 subunit (\u03b27). Additional modules important for the assembly of precursor complexes and their dimerization reside in the \u03b2 subunits themselves, either as transient or as permanent extensions. Particularly important domains are the propeptide of \u03b25 and the C-terminal extensions of \u03b22 and \u03b27. Upon maturation of the active sites by autocatalytic processing, UMP1 is degraded by the native proteasome.<\/jats:p>","DOI":"10.1042\/bst0380029","type":"journal-article","created":{"date-parts":[[2010,1,20]],"date-time":"2010-01-20T16:17:54Z","timestamp":1264004274000},"page":"29-33","update-policy":"https:\/\/doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":26,"title":["Chaperone-assisted assembly of the proteasome core particle"],"prefix":"10.1042","volume":"38","author":[{"given":"Ana\u00a0C.","family":"Matias","sequence":"first","affiliation":[{"name":"Institute for Genetics, University of Cologne, Z\u00fclpicher Strasse 47, D-50674 Cologne, Germany"},{"name":"Department of Biological Sciences and Bioenineering, University of Algarve, Faro, Portugal"},{"name":"Institute for Biotechnology and Bioengineering, Centre for Molecular and Structural Biomedicine, University of Algarve, Faro, Portugal"}]},{"given":"Paula\u00a0C.","family":"Ramos","sequence":"additional","affiliation":[{"name":"Department of Biological Sciences and Bioenineering, University of Algarve, Faro, Portugal"},{"name":"Institute for Biotechnology and Bioengineering, Centre for Molecular and Structural Biomedicine, University of Algarve, Faro, Portugal"}]},{"given":"R.","family":"J\u00fcrgen\u00a0Dohmen","sequence":"additional","affiliation":[{"name":"Institute for Genetics, University of Cologne, Z\u00fclpicher Strasse 47, D-50674 Cologne, Germany"}]}],"member":"288","published-online":{"date-parts":[[2010,1,19]]},"reference":[{"key":"2021111720282042300_B1","doi-asserted-by":"crossref","first-page":"1073","DOI":"10.1038\/80384","article-title":"The ubiquitin system","volume":"6","author":"Hershko","year":"2000","journal-title":"Nat. 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