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The yeast  Saccharomyces cerevisiae  is widely used as a cell factory to produce recombinant proteins. However,  S. cerevisiae  naturally secretes only a few proteins, such as invertase and the mating alpha factor, and its secretory capacity is limited. It has been reported that engineering protein anterograde trafficking from the endoplasmic reticulum to the Golgi apparatus by the moderate overexpression of  SEC16  could increase recombinant protein secretion in  S. cerevisiae . In this study, the retrograde trafficking in a strain with moderate overexpression of  SEC16  was engineered by overexpression of ADP-ribosylation factor GTP activating proteins, Gcs1p and Glo3p, which are involved in the process of COPI-coated vesicle formation. Engineering the retrograde trafficking increased the secretion of α-amylase but did not induce production of reactive oxygen species. An expanded ER membrane was detected in both the  GCS1  and  GLO3  overexpression strains. Physiological characterizations during batch fermentation showed that  GLO3  overexpression had better effect on recombinant protein secretion than  GCS1  overexpression. Additionally, the  GLO3  overexpression strain had higher secretion of two other recombinant proteins, endoglucanase I from  Trichoderma reesei  and glucan-1,4-α-glucosidase from  Rhizopus oryzae , indicating overexpression of  GLO3  in a  SEC16  moderate overexpression strain might be a general strategy for improving production of secreted proteins by yeast.   Electronic supplementary material  The online version of this article (10.1186/s13568-018-0571-x) contains supplementary material, which is available to authorized users.

Balanced trafficking between the ER and the Golgi apparatus increases protein secretion in yeast