Exiting the ER: what we know and what we don't.
The vast majority of proteins that are transported to different cellular compartments and secreted from the cell require coat protein complex II (COPII) for export from the endoplasmic reticulum (ER). Many of the molecular mechanisms underlying COPII assembly are understood in great detail, but it is becoming increasingly evident that this basic machinery is insufficient to account for diverse aspects of protein export from the ER that are observed in vivo. Here we review recent data that have furthered our mechanistic understanding of COPII assembly and, in particular, how genetic diseases associated with the early secretory pathway have added fundamental insights into the regulation of ER-derived carrier formation. We also highlight some unresolved issues that future work should address to better understand the physiology of COPII-mediated transport.
Telethon Institute of Genetics and Medicine, Via Pietro Castellino 111, Naples 80131, Italy.
Rossella
R
Venditti
Telethon Institute of Genetics and Medicine, Via Pietro Castellino 111, Naples 80131, Italy.
Cathal
C
Wilson
Telethon Institute of Genetics and Medicine, Via Pietro Castellino 111, Naples 80131, Italy. Electronic address: dematteis@tigem.it.
Maria Antonietta
MA
De Matteis
D000818:Animals; D022181:COP-Coated Vesicles / Q000378:metabolism; D004721:Endoplasmic Reticulum / Q000378:metabolism* / Q000648:ultrastructure; D006801:Humans; D009928:Organ Specificity; D021382:Protein Sorting Signals; D021381:Protein Transport; D022161:Transport Vesicles / Q000378:metabolism / Q000648:ultrastructure; D033921:Vesicular Transport Proteins / Q000378:metabolism
D021382:Protein Sorting Signals; C530638:SEC24A protein, human; D033921:Vesicular Transport Proteins
COPII coat; ER export; ER-derived carriers; genetic disease of membrane trafficking