Distinct isoform-specific complexes of TANGO1 cooperatively facilitate collagen secretion from the endoplasmic reticulum

Maeda, Miharu; Saito, Kota; Katada, Toshiaki

doi:10.1091/mbc.e16-03-0196

Cited by 49 publications

(100 citation statements)

References 21 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…One possibility is that starvation may further enhance the association between SEC12 and CTAGE5 to form a bigger protein complex which leads to the enlargement of SEC12-ERES. We analyzed the size of the SEC12-CTAGE5-TANGO1 complex by Blue Native-PAGE as described before [46]. We found that the size of the protein complex is not altered by starvation or PI3K inhibition ( Fig EV4), nor is the association between SEC12 and CTAGE5 in a co-IP experiment (Figs EV3A and 5 described later).…”

Section: Embo Reportsmentioning

confidence: 83%

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

et al. 2017

Self Cite

View full text Add to dashboard Cite

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.

show abstract

Section: Embo Reportsmentioning

confidence: 83%

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

et al. 2017

Self Cite

View full text Add to dashboard Cite

show abstract

“…Sec23a has been considered the target gene regulated by BBF2H7 for the formation of both regular and mega vesicles in mice (Supplemental Figure 6B) (18). In contract, Tango1 and Hsp47, regulated by BBF2H7, are known to be important in mega vesicle formation (17,30,31). Our results show that collagens but not regular cargo proteins, such as lysosomal enzymes, had defective ER-to-Golgi trafficking and secretion in the ER of the patient cells, suggesting that mega vesicle but not regular COP-II vesicle-mediated inter-organelle trafficking is impaired.…”

Section: Discussionmentioning

confidence: 99%

Site-1 protease deficiency causes human skeletal dysplasia due to defective inter-organelle protein trafficking

Fu¹,

Wang²,

Hoover³

et al. 2018

JCI Insight

View full text Add to dashboard Cite

“…In cells expressing TANGO1-∆PRD, the interaction between one of the 345 filament components, TANGO1, and the COPII subunits is abolished, indicating that, although 346 a TANGO1 filament could still be formed -this mutant does not alter the interaction between 347 TANGO1 and other TANGO1 or cTAGE5 proteins )-, the filament should 348 be less line-active because the affinity to bind to the peripheral COPII subunits is reduced. In 349 this situation the filament proteins cTAGE5 (Saito et al, 2011(Saito et al, , 2014) and TANGO1-Short 350 (Maeda, Saito and Katada, 2016) can still bind Sec23 and therefore reduce, albeit to a lesser 351 extent than in wild-type cells, the COPII patch line energy. However, in our results presented 352…”

Section: Introduction 37mentioning

confidence: 99%

A physical mechanism of TANGO1-mediated bulky cargo export

Raote

Chabanon

Walani

et al. 2019

Preprint

View full text Add to dashboard Cite

25The endoplasmic reticulum (ER)-resident transmembrane protein TANGO1 assembles 26 into rings around COPII subunits at ER exit sites (ERES), and links cytosolic membrane-27 remodeling machinery, tethers, and ER-Golgi intermediate compartment (ERGIC) mem-28 branes to procollagens in the ER lumen (Raote et al., 2018). This arrangement is proposed 29to create a direct route for transfer of procollagens from ERES to ERGIC membranes. 30Here, we present a physical model in which TANGO1 forms a linear filament that wraps 31around COPII lattices at ERES to stabilize the neck of a growing carrier on the cytoplas-32 mic face of the ER. Importantly, our results show that TANGO1 can induce the formation 33 of transport intermediates by regulating ER membrane tension. Altogether, our theoret-34ical approach provides a mechanical framework of how TANGO1 acts as a membrane 35 tension regulator to control procollagen export from the ER. 36 95 mation model. ERES consisting of COPII subunits assemble into in-plane circular lattices (orange), 96whereas proteins of the TANGO1 family assemble into filaments by lateral protein-protein interactions 97 (light blue). A tug-of-war between the affinity of the TANGO1 filament to bind COPII subunits (promoting 98 wetting) and the resistance of the filament to be bent (promoting dewetting) controls the wetting-dewetting 99 transition. Only when TANGO1 wets the COPII lattice, it acts as a linactant by stabilizing the peripheral 100 COPII subunits. 101 102 5

show abstract

Distinct isoform-specific complexes of TANGO1 cooperatively facilitate collagen secretion from the endoplasmic reticulum

Abstract: The short isoform of TANGO1, termed TANGO1S, is necessary for collagen secretion from the ER independently of TANGO1L. TANGO1L and TANGO1S form individual complexes at ER exit sites and cooperatively participate in collagen export from the ER.

Cited by 49 publications

References 21 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

Site-1 protease deficiency causes human skeletal dysplasia due to defective inter-organelle protein trafficking

A physical mechanism of TANGO1-mediated bulky cargo export

Contact Info

Product

Resources

About