{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,2,27]],"date-time":"2026-02-27T02:45:14Z","timestamp":1772160314051,"version":"3.50.1"},"reference-count":12,"publisher":"Wiley","issue":"13","license":[{"start":{"date-parts":[[2022,2,11]],"date-time":"2022-02-11T00:00:00Z","timestamp":1644537600000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by-nc-nd\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100001659","name":"Deutsche Forschungsgemeinschaft","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100001659","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["febs.onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["The FEBS Journal"],"published-print":{"date-parts":[[2022,7]]},"abstract":"<jats:p>\n                    RNA viruses in the\n                    <jats:italic>Picornaviridae<\/jats:italic>\n                    family express a large 250\u2009kDa viral polyprotein that is processed by virus\u2010encoded proteinases into mature functional proteins with specific functions for virus replication. One of these proteins is the highly conserved enteroviral transmembrane protein 3A that assists in reorganizing cellular membranes associated with the Golgi apparatus. Here, we studied the molecular properties of the Coxsackievirus B3 (CVB3) protein 3A with regard to its dimerization and its functional stability. By applying mutational analysis and biochemical characterization, we demonstrate that protein 3A forms DTT\u2010sensitive disulfide\u2010linked dimers via a conserved cytosolic cysteine residue at position 38 (Cys38). Homodimerization of CVB3 protein 3A via Cys38 leads to profound stabilization of the protein, whereas a C38A mutation promotes a rapid proteasome\u2010dependent elimination of its monomeric form. The lysosomotropic agent chloroquine (CQ) exerted only minor stabilizing effects on the 3A monomer but resulted in enrichment of the homodimer. Our experimental data demonstrate that disulfide linkages via a highly conserved Cys\u2010residue in enteroviral protein 3A have an important role in the dimerization of this viral protein, thereby preserving its stability and functional integrity.\n                  <\/jats:p>","DOI":"10.1111\/febs.16368","type":"journal-article","created":{"date-parts":[[2022,1,23]],"date-time":"2022-01-23T11:24:17Z","timestamp":1642937057000},"page":"3826-3838","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":3,"title":["A cytosolic disulfide bridge\u2010supported dimerization is crucial for stability and cellular distribution of Coxsackievirus B3 protein 3A"],"prefix":"10.1111","volume":"289","author":[{"given":"Martin","family":"Voss","sequence":"first","affiliation":[{"name":"Charit\u00e9 \u2013 Universit\u00e4tsmedizin Berlin, corporate member of Freie Universit\u00e4t Berlin and Humboldt\u2010Universit\u00e4t zu Berlin Institute of Biochemistry Berlin D\u201010117 Germany"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Gunnar","family":"Kleinau","sequence":"additional","affiliation":[{"name":"Charit\u00e9 \u2013 Universit\u00e4tsmedizin Berlin, corporate member of Freie Universit\u00e4t Berlin and Humboldt\u2010Universit\u00e4t zu Berlin Institute of Medical Physics and Biophysics, Group Protein X\u2010ray Crystallography and Signal Transduction Berlin Germany"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Niclas","family":"Gimber","sequence":"additional","affiliation":[{"name":"Charit\u00e9 \u2013 Universit\u00e4tsmedizin Berlin, corporate member of Freie Universit\u00e4t Berlin and Humboldt\u2010Universit\u00e4t zu Berlin AMBIO \u2010 Advanced Medical Bioimaging Core Facility Berlin Germany"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Katharina","family":"Janek","sequence":"additional","affiliation":[{"name":"Charit\u00e9 \u2013 Universit\u00e4tsmedizin Berlin, corporate member of Freie Universit\u00e4t Berlin and Humboldt\u2010Universit\u00e4t zu Berlin Institute of Biochemistry Berlin D\u201010117 Germany"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Clara","family":"Bredow","sequence":"additional","affiliation":[{"name":"Charit\u00e9 \u2013 Universit\u00e4tsmedizin Berlin, corporate member of Freie Universit\u00e4t Berlin and Humboldt\u2010Universit\u00e4t zu Berlin Institute of Biochemistry Berlin D\u201010117 Germany"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Fabien","family":"Thery","sequence":"additional","affiliation":[{"name":"Department of Biomolecular Medicine Ghent University  Belgium"},{"name":"VIB Center for Medical Biotechnology  Ghent Belgium"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Francis","family":"Impens","sequence":"additional","affiliation":[{"name":"Department of Biomolecular Medicine Ghent University  Belgium"},{"name":"VIB Center for Medical Biotechnology  Ghent Belgium"},{"name":"VIB Proteomics Core  Ghent Belgium"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Jan","family":"Schmoranzer","sequence":"additional","affiliation":[{"name":"Charit\u00e9 \u2013 Universit\u00e4tsmedizin Berlin, corporate member of Freie Universit\u00e4t Berlin and Humboldt\u2010Universit\u00e4t zu Berlin AMBIO \u2010 Advanced Medical Bioimaging Core Facility Berlin Germany"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-5028-2075","authenticated-orcid":false,"given":"Patrick","family":"Scheerer","sequence":"additional","affiliation":[{"name":"Charit\u00e9 \u2013 Universit\u00e4tsmedizin Berlin, corporate member of Freie Universit\u00e4t Berlin and Humboldt\u2010Universit\u00e4t zu Berlin Institute of Medical Physics and Biophysics, Group Protein X\u2010ray Crystallography and Signal Transduction Berlin Germany"},{"name":"Deutsches Zentrum f\u00fcr Herz\u2010Kreislauf\u2010Forschung 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