TY - JOUR TI - Ubiquitination drives COPI priming and Golgi SNARE localization AU - Date, Swapneeta S AU - Xu, Peng AU - Hepowit, Nathaniel L AU - Diab, Nicholas S AU - Best, Jordan AU - Xie, Boyang AU - Du, Jiale AU - Strieter, Eric R AU - Jackson, Lauren P AU - MacGurn, Jason A AU - Graham, Todd R A2 - Campelo, Felix A2 - Pfeffer, Suzanne R A2 - Campelo, Felix VL - 11 PY - 2022 DA - 2022/07/29 SP - e80911 C1 - eLife 2022;11:e80911 DO - 10.7554/eLife.80911 UR - https://doi.org/10.7554/eLife.80911 AB - Deciphering mechanisms controlling SNARE localization within the Golgi complex is crucial to understanding protein trafficking patterns within the secretory pathway. SNAREs are also thought to prime coatomer protein I (COPI) assembly to ensure incorporation of these essential cargoes into vesicles, but the regulation of these events is poorly understood. Here, we report roles for ubiquitin recognition by COPI in SNARE trafficking and in stabilizing interactions between Arf, COPI, and Golgi SNAREs in Saccharomyces cerevisiae. The ability of COPI to bind ubiquitin, but not the dilysine motif, through its N-terminal WD repeat domain of β′-COP or through an unrelated ubiquitin-binding domain is essential for the proper localization of Golgi SNAREs Bet1 and Gos1. We find that COPI, the ArfGAP Glo3, and multiple Golgi SNAREs are ubiquitinated. Notably, the binding of Arf and COPI to Gos1 is markedly enhanced by ubiquitination of these components. Glo3 is proposed to prime COPI–SNARE interactions; however, Glo3 is not enriched in the ubiquitin-stabilized SNARE–Arf–COPI complex but is instead enriched with COPI complexes that lack SNAREs. These results support a new model for how posttranslational modifications drive COPI priming events crucial for Golgi SNARE localization. KW - ubiquitin KW - membrane trafficking KW - COPI KW - Golgi biology KW - SNAREs KW - vesicle trafficking JF - eLife SN - 2050-084X PB - eLife Sciences Publications, Ltd ER -