ER-to-Golgi Carriers Arise through Direct En Bloc Protrusion and Multistage Maturation of Specialized ER Exit Domains

Mironov, Aleksandr; Beznoussenko, Galina V.; Trucco, Alvar; Lupetti, Pietro; Smith, Jeffrey D.; Geerts, Willie J. C.; Koster, Abraham J.; Burger, Koert N.J.; Martone, Maryann E.; Deerinck, Thomas J.; Ellisman, Mark H.; Luini, Alberto

doi:10.1016/s1534-5807(03)00294-6

Cited by 221 publications

(199 citation statements)

References 33 publications

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“…Although our data show that ECM secretion is dependent on the outer layer of the COPII coat, they do not preclude the possibility that ECM export from the ER, although COPIIdependent, might not in fact occur in COPII-coated carriers (Mironov et al, 2003). Such a model implies that the role of COPII is in trafficking of accessory factors that are required for cargo export, such as tethers and SNAREs.…”

Section: Discussionmentioning

confidence: 59%

Epithelial organization and cyst lumen expansion require efficient Sec13–Sec31-driven secretion

Townley

Schmidt

Hodgson

et al. 2012

Journal of Cell Science

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SummaryEpithelial morphogenesis is directed by interactions with the underlying extracellular matrix. Secretion of collagen and other matrix components requires efficient coat complex II (COPII) vesicle formation at the endoplasmic reticulum. Here, we show that suppression of the outer layer COPII component, Sec13, in zebrafish embryos results in a disorganized gut epithelium. In human intestinal epithelial cells (Caco-2), Sec13 depletion causes defective epithelial polarity and organization on permeable supports. Defects are seen in the ability of cells to adhere to the substrate, form a monolayer and form intercellular junctions. When embedded in a three-dimensional matrix, Sec13-depleted Caco-2 cells form cysts but, unlike controls, are defective in lumen expansion. Incorporation of primary fibroblasts within the three-dimensional culture substantially restores normal morphogenesis. We conclude that efficient COPIIdependent secretion, notably assembly of Sec13-Sec31, is required to drive epithelial morphogenesis in both two-and three-dimensional cultures in vitro, as well as in vivo. Our results provide insight into the role of COPII in epithelial morphogenesis and have implications for the interpretation of epithelial polarity and organization assays in cell culture.

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Section: Discussionmentioning

confidence: 59%

Epithelial organization and cyst lumen expansion require efficient Sec13–Sec31-driven secretion

Townley

Schmidt

Hodgson

et al. 2012

Journal of Cell Science

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“…A fourth, less well defined group of vesicles, transports procollagen from the ER to the Golgi (42). The procollagen transport vesicle may represent the third example of an ER to Golgi transport vesicle that does not require COPII proteins for ER budding (43). A fifth vesicle with a distinctive cargo, apolipoprotein-B100-associated very low density lipoprotein, appears to be COPII-dependent for budding from liver ER (44).…”

Section: Discussionmentioning

confidence: 99%

The Identification of a Novel Endoplasmic Reticulum to Golgi SNARE Complex Used by the Prechylomicron Transport Vesicle

Siddiqi

Mahan²,

Peggs

et al. 2006

Journal of Biological Chemistry

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Dietary long chain fatty acids are absorbed in the intestine, esterified to triacylglycerol, and packaged in the unique lipoprotein of the intestine, the chylomicron. The rate-limiting step in the transit of chylomicrons through the enterocyte is the exit of chylomicrons from the endoplasmic reticulum in prechylomicron transport vesicles (PCTV) that transport chylomicrons to the cis-Golgi. Because chylomicrons are 250 nm in average diameter and lipid absorption is intermittent, we postulated that a unique SNARE pairing would be utilized to fuse PCTV with their target membrane, cis-Golgi. PCTV loaded with [ 3 H]triacylglycerol were incubated with cis-Golgi and were separated from the Golgi by a sucrose step gradient. PCTV-chylomicrons acquire apolipoprotein-AI (apoAI) only after fusion with the Golgi. PCTV became isodense with Golgi upon incubation and were considered fused when their cargo chylomicrons acquired apoAI but docked when they did not. PCTV, docked with cis-Golgi, were solubilized in 2% Triton X-100, and proteins were immunoprecipitated using VAMP7 or rBet1 antibodies. In both cases, a 112-kDa complex was identified in nonboiled samples that dissociated upon boiling. The constituents of the complex were VAMP7, syntaxin 5, vti1a, and rBet1. Antibodies to each SNARE component significantly inhibited fusion of PCTV with cis-Golgi. Membrin, Sec22b, and Ykt6 were not found in the 112-kDa complex. We conclude that the PCTV-cisGolgi SNARE complex is composed of VAMP7, syntaxin 5, Bet1, and vti1a.

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“…After chain association, nucleation of the triple helix begins from the C-terminal-most Gly-X-Y repeats and propagates toward the N terminus in a zipper-like fashion. Later, folded collagen chains are translocated through the Golgi to the extracellular milieu via cisternal transport (Bonfanti et al 1998;Mironov et al 2003).…”

Section: Discussionmentioning

confidence: 99%

The C Terminus of Collagen SQT-3 Has Complex and Essential Functions in Nematode Collagen Assembly

Novelli

Page²,

Hodgkin

2006

Genetics

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The nematode exoskeleton is a multilayered structure secreted by the underlying hypodermal cells and mainly composed of small collagens, which are encoded by a large gene family. In previous work, we reported analysis of the C. elegans dpy-31 locus, encoding a hypodermally expressed zinc-metalloprotease of the BMP-1/TOLLOID family essential for viability and cuticle deposition. We have generated a large set of extragenic suppressors of dpy-31 lethality, most of which we show here to be allelic to the cuticle collagen genes sqt-3 and dpy-17. We analyzed the interaction among dpy-31, sqt-3, and dpy-17 using a SQT-3-specific antiserum, which was employed in immunofluorescence experiments. Our results support a role for DPY-31 in SQT-3 extracellular processing and suggest that the SQT-3 C-terminal nontrimeric region serves multiple roles during SQT-3 assembly. Different missense mutations of this region have diverse phenotypic consequences, including cold-sensitive lethality. Furthermore, the biochemical and genetic data indicate that the extracellular assemblies of DPY-17 and SQT-3 are interdependent, most likely because the collagens are incorporated into the same cuticular substructure. We find that absence of DPY-17 causes extensive intracellular retention of SQT-3, indicating that formation of the SQT-3-DPY-17 polymer could begin in the intracellular environment before secretion.

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ER-to-Golgi Carriers Arise through Direct En Bloc Protrusion and Multistage Maturation of Specialized ER Exit Domains

Cited by 221 publications

References 33 publications

Epithelial organization and cyst lumen expansion require efficient Sec13–Sec31-driven secretion

Epithelial organization and cyst lumen expansion require efficient Sec13–Sec31-driven secretion

The Identification of a Novel Endoplasmic Reticulum to Golgi SNARE Complex Used by the Prechylomicron Transport Vesicle

The C Terminus of Collagen SQT-3 Has Complex and Essential Functions in Nematode Collagen Assembly

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