Transport of soluble proteins through the Golgi occurs by diffusion via continuities across cisternae

Beznoussenko, Galina V.; Parashuraman, Seetharaman; Rizzo, Riccardo; Polishchuk, Roman; Martella, Oliviano; Giandomenico, Daniele Di; Fusella, Aurora; Spaar, Alexander; Sallese, Michele; Capestrano, Maria Grazia; Pavelka, Margit; Vos, Matthijn; Rikers, Yuri G M; Helms, Volkhard; Mironov, Alexandre; Luini, Alberto

doi:10.7554/elife.02009

Cited by 79 publications

(111 citation statements)

References 95 publications

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“…This model has been challenged. There have been reports on the formation of mega carriers, tubules, and direct and transient connections between cisternae, as well as rim progression, but there are no known specific molecular components that can be tested to validate their involvement and significance (Beznoussenko et al 2014, Glick & Nakano 2009, Lavieu et al 2013. In other words, the mechanism of general cargo export, and not just collagens, across the Golgi complex is still unclear.…”

Section: Trafficking Of Collagens Across the Golgi Complexmentioning

confidence: 93%

The Pathway of Collagen Secretion

Malhotra

Erlmann

2015

Annu. Rev. Cell Dev. Biol.

143

135

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COPII vesicles mediate export of secretory cargo from the endoplasmic reticulum (ER). However, a standard COPII vesicle with a diameter of 60-90 nm is too small to export collagens that are composed of rigid triple helices of up to 400 nm in length. How do cells pack and secrete such bulky molecules? This issue is fundamentally important, as collagens constitute approximately 25% of our dry body weight and are essential for almost all cell-cell interactions. Recently, a potential mechanism for the biogenesis of mega-transport carriers was identified, involving packing collagens and increasing the size of COPII coats. Packing is mediated by TANGO1, which binds procollagen VII in the lumen and interacts with the COPII proteins Sec23/Sec24 on the cytoplasmic side of the ER. Cullin3, an E3 ligase, and its specific adaptor protein, KLHL12, ubiquitinate Sec31, which could increase the size of COPII coats. Recruitment of these proteins and their specific interactors into COPII-mediated vesicle biogenesis may be all that is needed for the export of bulky collagens from the ER. Nonetheless, we present an alternative pathway in which TANGO1 and COPII cooperate to export collagens without generating a mega-transport carrier.

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Section: Trafficking Of Collagens Across the Golgi Complexmentioning

confidence: 93%

The Pathway of Collagen Secretion

Malhotra

Erlmann

2015

Annu. Rev. Cell Dev. Biol.

143

135

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“…Larger proteins, such as procollagen, are thought to traffic by a Golgi maturation-type mechanism, whereas smaller cargo appears to move either by vesicular transport or by diffusion through intercisternal tubular structures – narrow tunnel-like structures that connect individual cisternae (Beznoussenko et al, 2014). Labeling cargo proteins as well as Golgi resident proteins either green or red in two different cells that were subsequently fused revealed mixing of small Golgi proteins but not of large.…”

Section: Er and Golgi Anterograde And Retrograde Traffickingmentioning

confidence: 99%

Transcriptional regulation of secretory capacity by bZip transcription factors

Fox

Andrew

2014

Front. Biol.

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Cells of specialized secretory organs expand their secretory pathways to accommodate the increased protein load necessary for their function. The endoplasmic reticulum (ER), the Golgi apparatus and the secretory vesicles, expand not only the membrane components but also the protein machinery required for increased protein production and transport. Increased protein load causes an ER stress response akin to the Unfolded Protein Response (UPR). Recent work has implicated several bZip transcription factors in the regulation of protein components of the early secretory pathway necessary to alleviate this stress. Here, we highlight eight bZip transcription factors in regulating secretory pathway component genes. These include components of the three canonical branches of the UPR–ATF4, XBP1, and ATF6, as well as the five members of the Creb3 family of transcription factors. We review findings from both invertebrate and vertebrate model systems suggesting that all of these proteins increase secretory capacity in response to increased protein load. Finally, we propose that the Creb3 family of factors may have a dual role in secretory cell differentiation by also regulating the pathways necessary for cell cycle exit during terminal differentiation.

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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: 98%

“…Is trafficking of procollagen I by COPII vesicles [11], megacarriers [12] or by cisternal maturation [2]? Upon exiting the TGN, collagen I is excluded from CARTS [6].…”

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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Transport of soluble proteins through the Golgi occurs by diffusion via continuities across cisternae

Cited by 79 publications

References 95 publications

The Pathway of Collagen Secretion

The Pathway of Collagen Secretion

Transcriptional regulation of secretory capacity by bZip transcription factors

Procollagen export from the endoplasmic reticulum

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