[Cell Biology] Sorting and Export of Proteins at the Endoplasmic Reticulum

Ishier Raote1, Sonashree Saxena1 and Vivek Malhotra1,2,3 1Centre for Genomic Regulation (CRG), The Barcelona Institute of Science and Technology, Barcelona 08003, Spain 2Universitat Pompeu Fabra (UPF), Barcelona 08002, Spain 3ICREA, Barcelona 08010, Spain Correspondence: ishier.raotecrg.eu; vivek.malhotracrg.eu

Secretory proteins are transported from the endoplasmic reticulum (ER) to the Golgi complex in carriers that are formed by the concerted activities of cytoplasmic proteins in the coat protein complex II (COPII). COPII was first described in Saccharomyces cerevisiae and its basic functions are largely conserved throughout eukaryotes. The discovery of the TANGO1 (transport and Golgi organization 1) family of proteins is revealing insights into how cells can adapt COPII proteins to reorganize the ER exit site for the export of the most abundant and bulky molecules, collagens.

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