Study of Yeast Dop1 and Its Homologous DOPEY Proteins on Cellular Glycosylation and Vesicular Transport

Protein glycosylation is a conserved post-translational modification that is critical for various cellular phenomena. Structure similar glycosyltransferases or glycosidases cooperate to modify glycan structures in the Golgi of yeast or mammalian cells. The steady state localization of glycosyltransferases in the Golgi apparatus is influenced by vesicular transport and a variety of factors. This study explored the effect of Golgi peripheral protein Dop1 on cellular glycosylation. Live cell imaging by confocal fluorescence microscopy showed that Dop1 was predominantly localized to the late golgi apparatus. Both Dop1 and its interacting protein Neo1 (P4-ATPase) were involved in vesicular trafficking at the late golgi apparatus. In addition, Dop1 mediated the retrograde transport of Och1 glycosyltransferase. Furthermore, deletion of the mammalian Dop1 homologs DOPEY proteins led to changes in the structure of the Golgi, which weakly affected the glycosylation. Our results indicated that both yeast Dop1 and mammalian DOPEYs were involved in protein transport at the late stage of vesicular trafficking pathway and affected Golgi morphology or glycosylation.

CSTR: 32200.14.cjcb.2020.04.0011