{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,6]],"date-time":"2026-10-06T11:55:09Z","timestamp":1791287709760,"version":"4.1.0"},"reference-count":0,"publisher":"Oxford University Press (OUP)","license":[{"start":{"date-parts":[[2026,10,6]],"date-time":"2026-10-06T00:00:00Z","timestamp":1791244800000},"content-version":"am","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by-nc\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>Xyloglucan (XyGs), a plant-derived polysaccharide, supports gut health, is widely used as a food additive with stabilizing and gelling properties, and is increasingly being explored for drug delivery applications. XyG-synthesizing glycosyltransferases (GTs) are localized to Golgi, and their protein-protein interactions suggest the formation of multiprotein complexes; however, the mechanisms underlying protein complex assembly and transport, protein stability and degradation remain unknown. By employing the transient expression of YFP-fused GTs along with a cis-Golgi marker and generating fluorescence intensity profiles, we demonstrated the differential distribution of GTs in Golgi apparatus. The GTs half-lives were estimated using treatments with the protein synthesis inhibitor CHX. It was observed that the GTs exhibit distinct half-lives and, based on their turnover rates, display an apparent trend toward two groups. Our findings revealed that cellulose synthase-like C4 (CSLC4), galactosyltransferase (MUR3), and fucosyltransferase (FUT1) exhibit longer stability. In contrast, XyG xylosyltransferases XXT1, XXT2, XXT5, and galactosyltransferase XLT2 tend to have shorter half-lives. We also uncovered that protein-protein interactions among XyG-synthesizing GTs are not prerequisites for Golgi localization and our data are consistent with a model in which XyG-synthesizing GTs can reach the Golgi independently of their known interacting partners, exhibiting distinct sub-Golgi localization that shapes multiprotein complex assembly in specific cisternae. This spatial organization governs partner GT access and residence time for functional efficiency, while GT half-life variations regulate stability and interaction dynamics. Collectively, these factors provide a critical framework for independent operation and coordinated organization of Golgi-resident XyG-synthesizing proteins.<\/jats:p>","DOI":"10.1093\/pcp\/pcag139","type":"journal-article","created":{"date-parts":[[2026,10,3]],"date-time":"2026-10-03T11:39:21Z","timestamp":1791027561000},"source":"Crossref","is-referenced-by-count":0,"title":["Diverse Stability and Independent Trafficking of XyG-Synthesizing Glycosyltransferases in Distinct Golgi cisternae"],"prefix":"10.1093","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-4211-9865","authenticated-orcid":false,"given":"Ning","family":"Zhang","sequence":"first","affiliation":[{"name":"Roy J Carver Department of Biochemistry, Biophysics and Molecular Biology, Iowa State University , Ames, IA 50011 ,","place":["USA"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kayla","family":"Uthe","sequence":"additional","affiliation":[{"name":"Roy J Carver Department of Biochemistry, Biophysics and Molecular Biology, Iowa State University , Ames, IA 50011 ,","place":["USA"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Olga A","family":"Zabotina","sequence":"additional","affiliation":[{"name":"Roy J Carver Department of Biochemistry, Biophysics and Molecular Biology, Iowa State University , Ames, IA 50011 ,","place":["USA"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"286","published-online":{"date-parts":[[2026,10,6]]},"container-title":["Plant and Cell Physiology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/academic.oup.com\/pcp\/advance-article-pdf\/doi\/10.1093\/pcp\/pcag139\/71626272\/pcag139.pdf","content-type":"application\/pdf","content-version":"am","intended-application":"syndication"},{"URL":"https:\/\/academic.oup.com\/pcp\/advance-article-pdf\/doi\/10.1093\/pcp\/pcag139\/71626272\/pcag139.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,10,6]],"date-time":"2026-10-06T11:31:29Z","timestamp":1791286289000},"score":1,"resource":{"primary":{"URL":"https:\/\/academic.oup.com\/pcp\/advance-article\/doi\/10.1093\/pcp\/pcag139\/8868896"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,10,6]]},"references-count":0,"URL":"https:\/\/doi.org\/10.1093\/pcp\/pcag139","relation":{},"ISSN":["0032-0781","1471-9053"],"issn-type":[{"value":"0032-0781","type":"print"},{"value":"1471-9053","type":"electronic"}],"subject":[],"published":{"date-parts":[[2026,10,6]]},"article-number":"pcag139"}}