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Localization of low molecular weight GTP binding proteins to exocytic and endocytic compartments
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The ER-Golgi intermediate compartment (ERGIC): in search of its identity and function
TLDR
A stable compartment model in which ER-derived cargo is first shuttled from ER-exit sites to stationary ERGIC clusters in a COPII-dependent step and subsequently to the Golgi in a second vesicular transport step can better accommodate previous morphological and functional data on ER-to-Golgi traffic.
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Microtubule-dependent retrograde transport of proteins into the ER in the presence of brefeldin a suggests an ER recycling pathway
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Identification, by a monoclonal antibody, of a 53-kD protein associated with a tubulo-vesicular compartment at the cis-side of the Golgi apparatus
Purified Golgi membranes of the human intestinal adenocarcinoma cell line Caco-2 were used as an antigen to produce a monoclonal antibody, G1/93, which specifically labels a tubulovesicular…
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Giantin, a novel conserved Golgi membrane protein containing a cytoplasmic domain of at least 350 kDa.
TLDR
Giantin's localization, conservation, and physical properties suggest that it may participate in forming the intercisternal cross-bridges of the Golgi complex.
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ERGIC-53 and traffic in the secretory pathway.
TLDR
The ER-Golgi intermediate compartment (ERGIC) marker ERGIC-53 is a mannose-specific membrane lectin operating as a cargo receptor for the transport of glycoproteins from the ER to the ERG IC, an attractive probe for studying numerous aspects of protein trafficking in the secretory pathway.
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Role of Sec24 isoforms in selective export of membrane proteins from the endoplasmic reticulum
TLDR
The differential effects of Sec24 isoform‐specific silencing on the transport of the membrane reporter protein ERGIC‐53 (ER–Golgi intermediate compartment‐53) carrying the cytosolic ER export signals di‐phenylalanine, di‐tyrosine,di‐leucine,Di‐isoleucine‐ and valine‐mediated transport are reported.
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The lectin ERGIC-53 is a cargo transport receptor for glycoproteins
TLDR
It is shown that a cathepsin-Z-related glycoprotein binds to the recycling, mannose-specific membrane lectin ERGIC-53, indicating that ERG IC-53 may function as a receptor facilitating ER-to-ERGIC transport of soluble glycop protein cargo.
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Expression and intracellular transport of microvillus membrane hydrolases in human intestinal epithelial cells
TLDR
Results suggest that the major disaccharidases share a common biosynthetic mechanism that differs from that for peptidases, and indicate that the transport of microvillus membrane proteins to and through the Golgi apparatus is a selective process that may be mediated by transport receptors.
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Identification of an intermediate compartment involved in protein transport from endoplasmic reticulum to Golgi apparatus.
TLDR
The p53 compartment is established as the 15 degrees C intermediate of the endoplasmic reticulum-to-Golgi protein transport pathway.
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