
doi: 10.1242/jcs.100065
pmid: 22467862
Protein export from the endoplasmic reticulum (ER) to the Golgi apparatus occurs at specialized regions known as the ER exit sites (ERES). In Saccharomyces cerevisiae, ERES show numerous scattered puncta throughout the ER. We examined ERES localization within the peripheral ER, finding that ERES localize on high-curvature ER domains where curvature-stabilizing protein Rtn1 is present. Δrtn1 Δrtn2 Δyop1 cells have fewer high-curvature ER domains, but ERES accumulate at the remaining high-curvature ER domains on the edge of expanded ER sheets. We propose that membrane curvature is a key geometric feature for the regulation of ERES localization. We also investigated a spatial relationship between ERES and Golgi cisternae. Golgi cisternae in S. cerevisiae are unstacked, dispersed, and moving in the cytoplasm with cis-cisternae positioned adjacent to ERES, whereas trans-cisternae are not. Morphological changes in the ER of Δrtn1 Δrtn2 Δyop1 cells resulted in aberrant Golgi structures, including cis-and trans-markers, and exhibited reduced motion at ERES between expanded ER sheets and the plasma membrane.
Protein Transport, Saccharomyces cerevisiae Proteins, Microscopy, Fluorescence, Animals, Golgi Apparatus, Membrane Proteins, Intracellular Membranes, Saccharomyces cerevisiae, COP-Coated Vesicles, Endoplasmic Reticulum
Protein Transport, Saccharomyces cerevisiae Proteins, Microscopy, Fluorescence, Animals, Golgi Apparatus, Membrane Proteins, Intracellular Membranes, Saccharomyces cerevisiae, COP-Coated Vesicles, Endoplasmic Reticulum
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