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Peri-Golgi vesicles contain retrograde but not anterograde proteins consistent with the cisternal progression model of intra-Golgi transport.

Martinez-Menárguez JA, Prekeris R, Oorschot VM, Scheller R, Slot JW, Geuze HJ, Klumperman J - J. Cell Biol. (2001)

Bottom Line: A cisternal progression mode of intra-Golgi transport requires that Golgi resident proteins recycle by peri-Golgi vesicles, whereas the alternative model of vesicular transport predicts anterograde cargo proteins to be present in such vesicles.We found significant levels of the Golgi resident enzyme mannosidase II and the transport machinery proteins giantin, KDEL-receptor, and rBet1 in coatomer protein I-coated cisternal rims and peri-Golgi vesicles.By contrast, when cells expressed vesicular stomatitis virus protein G this anterograde marker was largely absent from the peri-Golgi vesicles.

View Article: PubMed Central - PubMed

Affiliation: Department of Cell Biology, School of Medicine, University of Murcia, 30071 Murcia, Spain.

ABSTRACT
A cisternal progression mode of intra-Golgi transport requires that Golgi resident proteins recycle by peri-Golgi vesicles, whereas the alternative model of vesicular transport predicts anterograde cargo proteins to be present in such vesicles. We have used quantitative immuno-EM on NRK cells to distinguish peri-Golgi vesicles from other vesicles in the Golgi region. We found significant levels of the Golgi resident enzyme mannosidase II and the transport machinery proteins giantin, KDEL-receptor, and rBet1 in coatomer protein I-coated cisternal rims and peri-Golgi vesicles. By contrast, when cells expressed vesicular stomatitis virus protein G this anterograde marker was largely absent from the peri-Golgi vesicles. These data suggest a role of peri-Golgi vesicles in recycling of Golgi residents, rather than an important role in anterograde transport.

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Man II colocalizes with giantin and KDELr in different populations of peri-Golgi vesicles. (A) Man II (10 nm gold) colocalizes with giantin (15 nm gold) in peri-Golgi vesicles (arrow). (B) Likewise, Man II (10 nm gold) is regularly found together with KDELr (15 nm gold) in peri-Golgi vesicles (arrows). (C) Despite the high labeling densities of both KDELr (10 nm gold) and giantin (15 nm gold), they are found mostly in different populations of peri-Golgi vesicles. Arrows point to KDELr-positive and giantin-negative vesicles. The arrowhead points to a Golgi cisternal rim that is strongly labeled KDELr and lacks giantin. G, Golgi complex. Bars, 200 nm.
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fig6: Man II colocalizes with giantin and KDELr in different populations of peri-Golgi vesicles. (A) Man II (10 nm gold) colocalizes with giantin (15 nm gold) in peri-Golgi vesicles (arrow). (B) Likewise, Man II (10 nm gold) is regularly found together with KDELr (15 nm gold) in peri-Golgi vesicles (arrows). (C) Despite the high labeling densities of both KDELr (10 nm gold) and giantin (15 nm gold), they are found mostly in different populations of peri-Golgi vesicles. Arrows point to KDELr-positive and giantin-negative vesicles. The arrowhead points to a Golgi cisternal rim that is strongly labeled KDELr and lacks giantin. G, Golgi complex. Bars, 200 nm.

Mentions: The membrane protein giantin is present in high concentrations in Golgi-derived COPI vesicles (Linstedt and Hauri, 1993; Sönnichsen et al., 1998) and has been implicated in intra-Golgi traffic. In NRK cells, giantin showed a consistent labeling pattern with the vast majority of label in the Golgi complex and associated vesicles (Fig. 5 and Fig. 6 A). In the Golgi complex itself, giantin was found over all cisternae with highest concentrations in G2–G4 (Table I). In agreement with its proposed function, 24% of Golgi-associated giantin was found in COPI-coated membranes (peri-Golgi vesicles and rims) and 18% in lateral rims on which no visible COPI coat was seen (Table II). Note that these values are in the same order as those for Man II.


Peri-Golgi vesicles contain retrograde but not anterograde proteins consistent with the cisternal progression model of intra-Golgi transport.

Martinez-Menárguez JA, Prekeris R, Oorschot VM, Scheller R, Slot JW, Geuze HJ, Klumperman J - J. Cell Biol. (2001)

Man II colocalizes with giantin and KDELr in different populations of peri-Golgi vesicles. (A) Man II (10 nm gold) colocalizes with giantin (15 nm gold) in peri-Golgi vesicles (arrow). (B) Likewise, Man II (10 nm gold) is regularly found together with KDELr (15 nm gold) in peri-Golgi vesicles (arrows). (C) Despite the high labeling densities of both KDELr (10 nm gold) and giantin (15 nm gold), they are found mostly in different populations of peri-Golgi vesicles. Arrows point to KDELr-positive and giantin-negative vesicles. The arrowhead points to a Golgi cisternal rim that is strongly labeled KDELr and lacks giantin. G, Golgi complex. Bars, 200 nm.
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Related In: Results  -  Collection

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fig6: Man II colocalizes with giantin and KDELr in different populations of peri-Golgi vesicles. (A) Man II (10 nm gold) colocalizes with giantin (15 nm gold) in peri-Golgi vesicles (arrow). (B) Likewise, Man II (10 nm gold) is regularly found together with KDELr (15 nm gold) in peri-Golgi vesicles (arrows). (C) Despite the high labeling densities of both KDELr (10 nm gold) and giantin (15 nm gold), they are found mostly in different populations of peri-Golgi vesicles. Arrows point to KDELr-positive and giantin-negative vesicles. The arrowhead points to a Golgi cisternal rim that is strongly labeled KDELr and lacks giantin. G, Golgi complex. Bars, 200 nm.
Mentions: The membrane protein giantin is present in high concentrations in Golgi-derived COPI vesicles (Linstedt and Hauri, 1993; Sönnichsen et al., 1998) and has been implicated in intra-Golgi traffic. In NRK cells, giantin showed a consistent labeling pattern with the vast majority of label in the Golgi complex and associated vesicles (Fig. 5 and Fig. 6 A). In the Golgi complex itself, giantin was found over all cisternae with highest concentrations in G2–G4 (Table I). In agreement with its proposed function, 24% of Golgi-associated giantin was found in COPI-coated membranes (peri-Golgi vesicles and rims) and 18% in lateral rims on which no visible COPI coat was seen (Table II). Note that these values are in the same order as those for Man II.

Bottom Line: A cisternal progression mode of intra-Golgi transport requires that Golgi resident proteins recycle by peri-Golgi vesicles, whereas the alternative model of vesicular transport predicts anterograde cargo proteins to be present in such vesicles.We found significant levels of the Golgi resident enzyme mannosidase II and the transport machinery proteins giantin, KDEL-receptor, and rBet1 in coatomer protein I-coated cisternal rims and peri-Golgi vesicles.By contrast, when cells expressed vesicular stomatitis virus protein G this anterograde marker was largely absent from the peri-Golgi vesicles.

View Article: PubMed Central - PubMed

Affiliation: Department of Cell Biology, School of Medicine, University of Murcia, 30071 Murcia, Spain.

ABSTRACT
A cisternal progression mode of intra-Golgi transport requires that Golgi resident proteins recycle by peri-Golgi vesicles, whereas the alternative model of vesicular transport predicts anterograde cargo proteins to be present in such vesicles. We have used quantitative immuno-EM on NRK cells to distinguish peri-Golgi vesicles from other vesicles in the Golgi region. We found significant levels of the Golgi resident enzyme mannosidase II and the transport machinery proteins giantin, KDEL-receptor, and rBet1 in coatomer protein I-coated cisternal rims and peri-Golgi vesicles. By contrast, when cells expressed vesicular stomatitis virus protein G this anterograde marker was largely absent from the peri-Golgi vesicles. These data suggest a role of peri-Golgi vesicles in recycling of Golgi residents, rather than an important role in anterograde transport.

Show MeSH
Related in: MedlinePlus