Concentration of Sec12 at ER exit sites via interaction with cTAGE5 is required for collagen export

Saito, Kota; Yamashiro, Koh; Shimazu, Noriko; Tanabe, Tomoya; Kontani, Kenji; Katada, Toshiaki

doi:10.1083/jcb.201312062

Cited by 96 publications

(159 citation statements)

References 36 publications

Supporting

Mentioning

145

Contrasting

Unclassified

Order By: Relevance

“…cTAGE5 binds TANGO1 with its second coiled-coil domain and, like TANGO1, the PRD of cTAGE5 interacts with SEC23A and SEC24C (Saito et al 2011). The first coiled-coil domain of cTAGE5 binds and recruits SEC12 to ERES without affecting SEC12-GEF activity (Saito et al 2014) (Figure 3b). Based on these data, it has been proposed that the binding of TANGO1 to PC VII in the lumen of the ER triggers TANGO1's PRD and that of its partner cTAGE5 to bind SEC23/24 (Figure 3b).…”

Section: Procollagen VII Export From the Endoplasmic Reticulum Requirmentioning

confidence: 96%

The Pathway of Collagen Secretion

Malhotra

Erlmann

2015

Annu. Rev. Cell Dev. Biol.

139

135

View full text Add to dashboard Cite

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.

show abstract

Section: Procollagen VII Export From the Endoplasmic Reticulum Requirmentioning

confidence: 96%

The Pathway of Collagen Secretion

Malhotra

Erlmann

2015

Annu. Rev. Cell Dev. Biol.

139

135

View full text Add to dashboard Cite

show abstract

“…cTAGE5 and TANGO1 interact through their second coiled-coil domain [20]. The first coiled-coil domain of cTAGE5 binds and recruits SEC12 to ER exit sites without affecting SEC12-GEF (guanine-nucleotideexchange factor) activity [21]. Knockdown of cTAGE5 by siRNA also arrests procollagen VII in the ER [20].…”

Section: Tango1 Is Required For Procollagen VII and Iv Export From Ermentioning

confidence: 98%

Procollagen export from the endoplasmic reticulum

Malhotra

Erlmann

Nogueira

2015

Biochemical Society Transactions

View full text Add to dashboard Cite

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.

show abstract

“…Expression of meningioma-expressed antigen 6 (Mea6), also known as cutaneous T cell lymphoma-associated antigen 5C (cTAGE5C), is upregulated in different tumor tissues or cell lines, and Mea6 is considered as an oncogene [22][23][24]. Mea6 has been shown to interact with transport and Golgi organization 1 (TANGO1) to facilitate collagen export from the cell [25][26][27][28]. Deletion of TANGO1 in mice results in defects in collagen secretion similar to the phenotype associated with defect in COPII function [29,30].…”

Section: Introductionmentioning

confidence: 99%

Mea6 controls VLDL transport through the coordinated regulation of COPII assembly

et al. 2016

View full text Add to dashboard Cite

Lipid accumulation, which may be caused by the disturbance in very low density lipoprotein (VLDL) secretion in the liver, can lead to fatty liver disease. VLDL is synthesized in endoplasmic reticulum (ER) and transported to Golgi apparatus for secretion into plasma. However, the underlying molecular mechanism for VLDL transport is still poorly understood. Here we show that hepatocyte-specific deletion of meningioma-expressed antigen 6 (Mea6)/cutaneous T cell lymphoma-associated antigen 5C (cTAGE5C) leads to severe fatty liver and hypolipemia in mice. Quantitative lipidomic and proteomic analyses indicate that Mea6/cTAGE5 deletion impairs the secretion of different types of lipids and proteins, including VLDL, from the liver. Moreover, we demonstrate that Mea6/cTAGE5 interacts with components of the ER coat protein complex II (COPII) which, when depleted, also cause lipid accumulation in hepatocytes. Our findings not only reveal several novel factors that regulate lipid transport, but also provide evidence that Mea6 plays a critical role in lipid transportation through the coordinated regulation of the COPII machinery.

show abstract

Concentration of Sec12 at ER exit sites via interaction with cTAGE5 is required for collagen export

Abstract: By interacting with the collagen cargo receptor component cTAGE5, Sec12 concentrates at ER exit sites and generates the high levels of GTP-bound Sar1 necessary for export of collagen to the Golgi.

Cited by 96 publications

References 36 publications

The Pathway of Collagen Secretion

The Pathway of Collagen Secretion

Procollagen export from the endoplasmic reticulum

Mea6 controls VLDL transport through the coordinated regulation of COPII assembly

Contact Info

Product

Resources

About