Diverse Stability and Independent Trafficking of XyG-Synthesizing Glycosyltransferases in Distinct Golgi cisternae

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ID: 331699
2026
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Abstract
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.
Reference Key
openalex_W7220649815 Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors Ning Zhang, Kayla Uthe, Olga A. Zabotina
Journal plant and cell physiology
Year 2026
DOI
10.1093/pcp/pcag139
URL
https://doi.org/10.1093/pcp/pcag139
Keywords Keywords not found

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