Dual function of cTAGE5 in collagen export from the endoplasmic reticulum

Tanabe, Tomoya; Maeda, Miharu; Saito, Kota; Katada, Toshiaki

doi:10.1091/mbc.e16-03-0180

Cited by 34 publications

(36 citation statements)

References 18 publications

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“…For example, in the event of large cargo secretion (collagen VII), SEC12 concentration on the ERES via association with CTAGE5 is required for large cargo export out of the ER [43]. Concentration of SEC12 may facilitate the efficient activation of SAR1 to enhance the packaging of large cargoes [57]. Our study further suggests that the concentration of SEC12 on the ERES facilitates its relocation to the ERGIC to trigger the assembly of ERGIC-COPII vesicles and thus autophagosome biogenesis (Fig 2, 3).…”

Section: Discussionmentioning

confidence: 99%

Remodeling of ER-exit sites initiates a membrane supply pathway for autophagosome biogenesis

Zhang

Kenny

et al. 2017

Preprint

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Autophagosomes are double-membrane vesicles generated during autophagy. Biogenesis of the autophagosome requires membrane acquisition from intracellular compartments, the mechanisms of which are unclear. We previously found that a relocation of COPII machinery to the ER-Golgi intermediate compartment (ERGIC) generates ERGIC-derived COPII vesicles which serve as a membrane precursor for the lipidation of LC3, a key membrane component of the autophagosome. Here we employed super-resolution microscopy to show that starvation induces the enlargement of ER-exit sites (ERES) positive for the COPII activator, SEC12, and the remodeled ERES patches along the ERGIC. A SEC12 binding protein, CTAGE5, is required for the enlargement of ERES, SEC12 relocation to the ERGIC, and modulates autophagosome biogenesis. Moreover, FIP200, a subunit of the ULK protein kinase complex, facilitates the starvation-induced enlargement of ERES independent of the other subunits of this complex and associates via its C-terminal domain with SEC12. Our data indicate a pathway wherein FIP200 and CTAGE5 facilitate starvation-induced remodeling of the ERES, a prerequisite for the production of COPII vesicles budded from the ERGIC that contribute to autophagosome formation. Running title: Endomembrane remodeling for autophagy

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Section: Discussionmentioning

confidence: 99%

Remodeling of ER-exit sites initiates a membrane supply pathway for autophagosome biogenesis

Zhang

Kenny

et al. 2017

Preprint

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“…S1). The importance of a high concentration of activated SAR1 during large cargo secretion was demonstrated in another recent report, where overexpression of wild-type SAR1 but not the GTP locked H79G mutant rescued secretion of collagen VII in cells where the localization of SEC12 was dispersed as a result of cTAGE5 knockdown (37).…”

Section: Discussionmentioning

confidence: 89%

“…As the first step of COPII formation, SAR1 is recruited to the ER membrane by its GEF SEC12 (29), and the subsequent nucleotide exchange exposes an amphipathic helix which intercalates into the ER membrane, thereby inducing membrane curvature (3,4). Activated SAR1-GTP recruits the inner coat proteins SEC23/24, where SEC23 is the GTPase activating protein (GAP) for SAR1 (37). The inner coat proteins then recruit the outer coat proteins SEC13/31, where SEC31 acts to stimulate the GAP activity of SEC23 a further 10-fold (5).…”

Section: Discussionmentioning

confidence: 99%

TANGO1 and SEC12 are co-packaged with procollagen I to facilitate the generation of large COPII carriers

Yuan

Kenny

Hemmati

et al. 2018

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Large COPII-coated vesicles serve to convey the large cargo procollagen I (PC1) from the endoplasmic reticulum (ER). The link between large cargo in the lumen of the ER and modulation of the COPII machinery remains unresolved. TANGO1 is required for procollagen (PC) secretion and interacts with PC and COPII on opposite sides of the ER membrane, but evidence suggests that TANGO1 is retained in the ER, and not included in normal size (<100nm) COPII vesicles. Here we show that TANGO1 is exported out of the ER in large COPII-coated PC1 carriers, and retrieved back to the ER by the retrograde coat, COPI, mediated by the C-terminal RDEL retrieval sequence of HSP47. TANGO1 is known to target the COPII initiation factor SEC12 to ER exit sites through an interacting protein, cTAGE5. SEC12 is important for the growth of COPII vesicles, but it is not sorted into small budded vesicles. We found both cTAGE5 and SEC12 were exported with TANGO1 in large COPII carriers. In contrast to its exclusion from small transport vesicles, SEC12 was particularly enriched around ER membranes and large COPII carriers that contained PC1. We constructed a split GFP system to recapitulate the targeting of SEC12 to PC1 via the luminal domain of TANGO1. The minimal targeting system enriched SEC12 around PC1 and generated large PC1 carriers. We conclude that TANGO1, cTAGE5, and SEC12 are co-packed with PC1 into COPII carriers to increase the size of COPII thus ensuring the capture of large cargo.

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“…Positive hybridoma lines were subcloned, grown in serum-free medium (Nihon Pharmaceutical) supplemented with hypoxanthine-thymidine (Thermo Fisher Scientific), and purified with protein G-Sepharose (GE Healthcare; Saito et al, 2014). Polyclonal antibodies against Sec16-N (374–387 aa), Sec16-C (2,319–2,332 aa), and TANGO1-CT (1,884–1,898 aa for TANGO1L; 762–776 aa for TANGO1S) were raised in rabbits by immunization with keyhole limpet hemocyanin-conjugated peptides and affinity-purified by columns conjugated with the peptides (Thermo Fisher Scientific; Iinuma et al, 2007; Saito et al, 2009, 2011; Maeda et al, 2016; Tanabe et al, 2016). Polyclonal antibodies against Sec31 and TANGO1-CC1 were raised in rabbits by immunization with recombinant Sec31 (522-719 aa) or GST-tagged TANGO1L (1,231–1,340 aa) [TANGO1S (109–218 aa)] and affinity-purified by columns conjugated with GST-tagged Sec31 (522-719 aa) or ColdTF-tagged TANGO1 (1,231–1,340 aa) [TANGO1S (109–218 aa)] (Saito et al, 2011; Tanabe et al, 2016).…”

Section: Methodsmentioning

confidence: 99%

“…Polyclonal antibodies against Sec16-N (374–387 aa), Sec16-C (2,319–2,332 aa), and TANGO1-CT (1,884–1,898 aa for TANGO1L; 762–776 aa for TANGO1S) were raised in rabbits by immunization with keyhole limpet hemocyanin-conjugated peptides and affinity-purified by columns conjugated with the peptides (Thermo Fisher Scientific; Iinuma et al, 2007; Saito et al, 2009, 2011; Maeda et al, 2016; Tanabe et al, 2016). Polyclonal antibodies against Sec31 and TANGO1-CC1 were raised in rabbits by immunization with recombinant Sec31 (522-719 aa) or GST-tagged TANGO1L (1,231–1,340 aa) [TANGO1S (109–218 aa)] and affinity-purified by columns conjugated with GST-tagged Sec31 (522-719 aa) or ColdTF-tagged TANGO1 (1,231–1,340 aa) [TANGO1S (109–218 aa)] (Saito et al, 2011; Tanabe et al, 2016). Other antibodies were as follows: CK1δ (rabbit; Proteintech), CK1ε (mouse; BD), PPP1CA (mouse; Santa Cruz), PPP1CB (mouse; Santa Cruz), GAPDH (mouse; Merck), FLAG (mouse; Merck), FLAG (rat; agilent), HA (rat; Roche), and Sec31 (mouse; BD).…”

Section: Methodsmentioning

confidence: 99%

Mitotic ER exit site dissociation and reassembly is regulated by TANGO1 phosphorylation status

Maeda

Komatsu

Saito

2019

Preprint

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1Golgi fragmentation and ER exit site dissociation are considered as the leading 2 causes of mitotic block of secretion from the ER. Although the mechanisms of Golgi 3 fragmentation have been extensively characterized, ER exit block early in mitosis is 4 not well-understood. We previously found that TANGO1 organizes ER exit sites by 5 directly interacting with Sec16. Here, we showed that TANGO1 is phosphorylated 6 by casein kinase 1 (CK1) during mitosis. Interestingly, the interaction with Sec16 7 was abrogated by phosphorylation of TANGO1, leading to dissociation of the ER 8 exit sites. Moreover, a TANGO1 mutant deficient in phosphorylation inhibited the 9 mitotic dissociation of ER exit sites. In contrast, a TANGO1 mutant mimicking 10 CK1-mediated phosphorylation dissociated ER exit sites in interphase cells. 11

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Dual function of cTAGE5 in collagen export from the endoplasmic reticulum

Cited by 34 publications

References 18 publications

Remodeling of ER-exit sites initiates a membrane supply pathway for autophagosome biogenesis

Remodeling of ER-exit sites initiates a membrane supply pathway for autophagosome biogenesis

TANGO1 and SEC12 are co-packaged with procollagen I to facilitate the generation of large COPII carriers

Mitotic ER exit site dissociation and reassembly is regulated by TANGO1 phosphorylation status

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