Cytosolic Ca²⁺ Modulates Golgi Structure Through PKCα-Mediated GRASP55 Phosphorylation.

ABSTRACT: It has been well documented that the ER responds to cellular stresses through the unfolded protein response (UPR), but it is unknown how the Golgi responds to similar stresses. In this study, we treated HeLa cells with ER stress inducers, thapsigargin (TG), tunicamycin (Tm), and dithiothreitol (DTT), and found that only TG treatment resulted in Golgi fragmentation. TG induced Golgi fragmentation at a low dose and short time when UPR was undetectable, indicating that Golgi fragmentation occurs independently of ER stress. Further experiments demonstrated that TG induces Golgi fragmentation through elevating intracellular Ca²⁺ and protein kinase Cα (PKCα) activity, which phosphorylates the Golgi stacking protein GRASP55. Significantly, activation of PKCα with other activating or in

SUBMITTER: Ireland S 

PROVIDER: S-EPMC7078314 | biostudies-literature | 2020 Mar

REPOSITORIES: biostudies-literature