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The ER-Golgi intermediate compartment (ERGIC): in search of its identity and function
Protein traffic moving from the endoplasmic reticulum (ER) to the Golgi complex in mammalian cells passes through the tubulovesicular membrane clusters of the ER-Golgi intermediate compartmentExpand
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Role of Sec24 isoforms in selective export of membrane proteins from the endoplasmic reticulum
Sec24 of the COPII (coat protein complex II) vesicle coat mediates the selective export of membrane proteins from the endoplasmic reticulum (ER) in yeast. Human cells express four Sec24 isoforms, butExpand
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The lectin ERGIC-53 is a cargo transport receptor for glycoproteins
Soluble secretory proteins are transported from the endoplasmic reticulum (ER) to the ER–Golgi intermediate compartment (ERGIC) in vesicles coated with COP-II coat proteins. The sorting of secretoryExpand
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Selective export of human GPI-anchored proteins from the endoplasmic reticulum
Selective export of transmembrane proteins from the endoplasmic reticulum (ER) relies on recognition of cytosolic-domain-localized transport signals by the Sec24 subunit of the COPII vesicle coat.Expand
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Phosphorylation controls CLIMP-63-mediated anchoring of the endoplasmic reticulum to microtubules.
The microtubule-binding 63-kDa cytoskeleton-linking membrane protein (CLIMP-63) is an integral membrane protein that links the endoplasmic reticulum (ER) to microtubules. Here, we tested whether thisExpand
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Adaptation of endoplasmic reticulum exit sites to acute and chronic increases in cargo load
The biogenesis of endoplasmic reticulum (ER) exit sites (ERES) involves the formation of phosphatidylinositol‐4 phosphate (PI4) and Sec16, but it is entirely unknown how ERES adapt to variations inExpand
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The Emp24 Complex Recruits a Specific Cargo Molecule into Endoplasmic Reticulum–Derived Vesicles
Members of the yeast p24 family, including Emp24p and Erv25p, form a heteromeric complex required for the efficient transport of selected proteins from the endoplasmic reticulum (ER) to the GolgiExpand
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MAPK signaling to the early secretory pathway revealed by kinase/phosphatase functional screening
An RNAi screen determines that the early secretory pathway is subject to phosphoregulation via a variety of signaling pathways, including a link between growth factor signaling and ER export.
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Role of cytoplasmic C-terminal amino acids of membrane proteins in ER export.
Export of membrane proteins from the ER is believed to be selective and require transport signals, but the identity of such signals has remained elusive. The recycling type I membrane proteinExpand
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Capturing protein interactions in the secretory pathway of living cells.
The secretory pathway is composed of membrane compartments specialized in protein folding, modification, transport, and sorting. Numerous transient protein-protein interactions guide theExpand
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