Department of Cell Biology and Howard Hughes Medical Institute, Yale University School of Medicine, New Haven, CT 06510, USA-
Abstract: The endoplasmic reticulum -ER- contains both cisternal and reticular elements in one contiguous structure- We identified rtn1Delta in a systematic screen for yeast mutants with altered ER morphology- The ER in rtn1Delta cells is predominantly cisternal rather than reticular, yet the net surface area of ER is not significantly changed- Rtn1-green fluorescent protein -GFP- associates with the reticular ER at the cell cortex and with the tubules that connect the cortical ER to the nuclear envelope, but not with the nuclear envelope itself- Rtn1p overexpression also results in an altered ER structure- Rtn proteins are found on the ER in a wide range of eukaryotes and are defined by two membrane-spanning domains flanking a conserved hydrophilic loop- Our results suggest that Rtn proteins may direct the formation of reticulated ER- We independently identified Rtn1p in a proteomic screen for proteins associated with the exocyst vesicle tethering complex- The conserved hydophilic loop of Rtn1p binds to the exocyst subunit Sec6p- Overexpression of this loop results in a modest accumulation of secretory vesicles, suggesting impaired exocyst function- The interaction of Rtn1p with the exocyst at the bud tip may trigger the formation of a cortical ER network in yeast buds-