The Golgi ribbon structure facilitates anterograde transport of large cargoes

The Golgi complex is responsible for processing and sorting of secretory cargos. Microtubules are known to accelerate the transport of proteins from the endoplasmic reticulum (ER) to the Golgi complex and from the Golgi to the plasma membrane. However, whether postGolgi transport strictly requires microtubules is still unclear. Using the retention using selective hooks (RUSH) system to synchronize the trafficking of cargos, we show that anterograde transport of tumor necrosis factor (TNF) is strongly reduced without microtubules. We show that two populations of Golgi elements co-exist in these cells. A centrally located and giantin-positive Golgi complex that sustains trafficking, and newly formed peripheral Golgi mini-stacks that accumulate cargos in cells without microtubules. Using a genomeedited GFP-giantin cell line, we observe that the trafficking-competent Golgi population corresponds to the pre-existing population that was present before removal of microtubules. All Golgi elements support trafficking after long-term depletion of microtubules and after relocation of Golgi proteins to the ER after treatment with Brefeldin A. Our results demonstrate that functional maturation of Golgi elements is needed to ensure post-Golgi trafficking, and that microtubule-driven post-Golgi transport is not strictly required.

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“…important for particular cargos, such as large cargos as recently suggested (Ferraro et al, 2014;Lavieu et al, 2014).…”

Section: Role Of Microtubules In Golgi-dependent Transportmentioning

confidence: 99%

Microtubule-independent secretion requires functional maturation of Golgi elements

Fourrière

Divoux

Roceri

et al. 2016

Journal of Cell Science

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“…Trafficking of cargoes across the Golgi is a contentious topic. There is data on the involvement of COPI vesicles, tubules, continuities across the cisternae of the Golgi stacks and cargo transport by non-vesicular or cisternal maturation [2][3][4][5]. Export of proteins from late Golgi for secretion or delivery to the PM is mediated by a number of distinct carriers and those that have been described in greater detail include carriers of the trans-Golgi network (TGN) to the cell surface (CARTS) [6] and clathrin-coated vesicles [7].…”

Section: Introductionmentioning

confidence: 99%

Procollagen export from the endoplasmic reticulum

Malhotra

Erlmann

Nogueira

2015

Biochemical Society Transactions

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Collagens are secreted into the extracellular space where they assemble into a large complex protein network to form basement membrane and extracellular matrix. Collagens are therefore essential for cell attachment, tissue organization and the overall survival of all multicellular organisms. Collagens are synthesized in the endoplasmic reticulum (ER) but they are too big to fit into a conventional coat protein complex II (COPII) transport carrier of 60-90 nm average diameter. How are these molecules exported from the ER and then transported along the secretory pathway? We describe here the involvement of special packing machinery composed of hetero oligomers of transport and Golgi organization 1 (TANGO1) and cutaneous T-cell lymphoma-associated antigen 5 (cTAGE5) in the export of procollagen VII from the ER.

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“…The exception are vertebrates, where the stacks are laterally connected to form a contiguous ribbon-like structure that is positioned in close proximity to the centrosomes in the perinuclear region of the cell (3). On one hand, the interconnection of cisternae facilitates the accommodation and processing of large cargos such as collagen (4,5). On the other hand, the close positioning of the Golgi ribbon to the centrosomes guides membrane traffic for polarized secretion and thus plays a pivotal role in cell polarization (6)(7)(8).…”

mentioning

confidence: 99%

Mitotic Golgi disassembly is required for bipolar spindle formation and mitotic progression

Guizzunti

Seemann

2016

Proc. Natl. Acad. Sci. U.S.A.

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During mitosis, the mammalian Golgi vesiculates and, upon partitioning, reassembles in each daughter cell; however, it is not clear whether the disassembly process per se is important for partitioning or is merely an outcome of mitotic entry. Here, we show that Golgi vesiculation is required for progression to metaphase. To prevent Golgi disassembly, we expressed HRP linked to a Golgi-resident protein and acutely triggered the polymerization of 3,3′-diaminobenzidine (DAB) in the Golgi lumen. The DAB polymer does not affect interphase cell viability, but inhibits Golgi fragmentation by nocodazole and brefeldin A and also halts cells in early mitosis. The arrest is Golgi specific and does not occur when DAB is polymerized in the endosomes. Cells with a DAB polymer in the Golgi enter mitosis normally but arrest with an intact Golgi clustered at a monopolar spindle and an active spindle assembly checkpoint (SAC). Mitotic progression is restored upon centrosome depletion by the Polo-like kinase 4 inhibitor, centrinone, indicating that the link between the Golgi and the centrosomes must be dissolved to reach metaphase. These results demonstrate that Golgi disassembly is required for mitotic progression because failure to vesiculate the Golgi activates the canonical SAC. This requirement suggests that cells actively monitor Golgi integrity in mitosis.

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The Golgi ribbon structure facilitates anterograde transport of large cargoes

Abstract: Breaking down the ribbon of mammalian cells strongly inhibits intra-Golgi transport of large cargoes without altering the rate of transport of smaller cargoes. These results imply that the ribbon structure is an essential requirement for transport of large cargoes in mammalian cells.

Cited by 56 publications

References 41 publications

Microtubule-independent secretion requires functional maturation of Golgi elements

Microtubule-independent secretion requires functional maturation of Golgi elements

Procollagen export from the endoplasmic reticulum

Mitotic Golgi disassembly is required for bipolar spindle formation and mitotic progression

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