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Upon glucose withdrawal, the soluble GET proteins re-localize to dynamic cytosolic foci, here termed GET bodies. Our data reveal that the pre-targeting complex components, Sgt2 and the Get4\u2013Get5 heterodimer, and the Get3 ATPase play important roles in the assembly of these structures in Saccharomyces cerevisiae. More specifically, the TPR region of Sgt2 is required as a GET body scaffold. Systematic compositional analyses of GET bodies reveal their chaperone-rich nature and the presence of numerous proteins involved in metabolic processes. Temporal analyses of GET body assembly demonstrate the sequential recruitment of different chaperones, and we discover the requirement of Sis1 and Sti1 for maintaining the dynamic properties of these structures. In vivo, NADH derived from the oxidation of ethanol to acetaldehyde can induce GET body disassembly in a reaction depending on the alcohol dehydrogenase Adh2 and in vitro, addition of NADH resolves GET bodies. This suggests a mechanistic basis for their formation and disassembly in response to the metabolic shift caused by glucose withdrawal and re-addition.<\/jats:p>","DOI":"10.1242\/jcs.263616","type":"journal-article","created":{"date-parts":[[2025,2,20]],"date-time":"2025-02-20T15:08:51Z","timestamp":1740064131000},"source":"Crossref","is-referenced-by-count":2,"title":["The formation of chaperone-rich GET bodies depends on the tetratricopeptide repeat region of Sgt2 and is reversed by NADH"],"prefix":"10.1242","volume":"138","author":[{"ORCID":"https:\/\/orcid.org\/0009-0003-4227-4165","authenticated-orcid":false,"given":"Jonas","family":"Jennrich","sequence":"first","affiliation":[{"name":"University Medical Centre G\u00f6ttingen 1 Department of Molecular Biology , , Justus-von-Liebig-Weg 11, 37077 G\u00f6ttingen ,","place":["Germany"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-7295-3391","authenticated-orcid":false,"given":"\u00c1kos","family":"Farkas","sequence":"additional","affiliation":[{"name":"University Medical Centre G\u00f6ttingen 1 Department of Molecular Biology , , Justus-von-Liebig-Weg 11, 37077 G\u00f6ttingen ,","place":["Germany"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-1837-5233","authenticated-orcid":false,"given":"Henning","family":"Urlaub","sequence":"additional","affiliation":[{"name":"Max Planck Institute for Multidisciplinary Sciences, Bioanalytical Mass Spectrometry 2 , Am Fa\u00dfberg 11, 37077 G\u00f6ttingen ,","place":["Germany"]},{"name":"Institute for Clinical Chemistry, University Medical Centre G\u00f6ttingen 3 , Robert-Koch-Stra\u00dfe 40, 35075 G\u00f6ttingen ,","place":["Germany"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Blanche","family":"Schwappach","sequence":"additional","affiliation":[{"name":"University Medical Centre G\u00f6ttingen 1 Department of Molecular Biology , , Justus-von-Liebig-Weg 11, 37077 G\u00f6ttingen ,","place":["Germany"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-6035-4255","authenticated-orcid":false,"given":"Katherine E.","family":"Bohnsack","sequence":"additional","affiliation":[{"name":"University Medical Centre G\u00f6ttingen 1 Department of Molecular Biology , , Justus-von-Liebig-Weg 11, 37077 G\u00f6ttingen ,","place":["Germany"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"237","published-online":{"date-parts":[[2025,3,20]]},"reference":[{"key":"2025032007030648000_JCS263616C111","doi-asserted-by":"publisher","first-page":"e52956","DOI":"10.1371\/journal.pone.0052956","article-title":"Nuclear import of UBL-domain protein Mdy2 is required for heat-induced stress response in Saccharomyces cerevisiae","volume":"7","author":"Arhzaouy","year":"2012","journal-title":"PLoS One"},{"key":"2025032007030648000_JCS263616C1","doi-asserted-by":"publisher","first-page":"1134","DOI":"10.1016\/j.cell.2013.02.003","article-title":"A network of cytosolic factors targets SRP-independent proteins to the endoplasmic reticulum","volume":"152","author":"Ast","year":"2013","journal-title":"Cell"},{"key":"2025032007030648000_JCS263616C2","doi-asserted-by":"publisher","first-page":"4079","DOI":"10.1242\/jcs.204396","article-title":"Targeting and translocation of proteins to the endoplasmic reticulum at a glance","volume":"130","author":"Aviram","year":"2017","journal-title":"J. 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