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Significance The unfolded protein response (UPR) is a cellular response to stress caused by accumulation of unfolded or misfolded proteins in the endoplasmic reticulum lumen. ADP ribosylation factor (Arf) GTPases are key regulators of membrane traffic in the Golgi complex. In yeast, Arf guanine nucleotide-exchange factor (GEF) Syt1p activates the Arf-like protein Arl1 at late Golgi, thereby recruiting golgin Imh1p, but how Syt1p GEF activity is regulated is largely unknown. We demonstrate that UPR signaling regulated phosphorylation of Syt1, which is critical for Arl1p activation, recruitment of golgin protein Imh1p to the Golgi, and Syt1p interaction with Arl1. These findings reveal a previously unsuspected relationship between the UPR and Golgi transport.

Unfolded protein response regulates yeast small GTPase Arl1p activation at late Golgi via phosphorylation of Arf GEF Syt1p