Tango1 spatially organizes ER exit sites to control ER export

Liu, Min; Feng, Zhi Jing; Ke, Hongmei; Liu, Ying; Sun, Tianhui; Dai, Jianli; Cui, Wenhong; Pastor-Pareja, José Carlos

doi:10.1083/jcb.201611088

Cited by 80 publications

(163 citation statements)

References 67 publications

(81 reference statements)

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“…In particular, it is difficult to reconcile how the association between TFG and Sec23 would be restricted to large transport carriers. Additionally, early embryo lethality observed upon TFG knockout in rodents is inconsistent with the more subtle impacts of deleting receptors known to regulate the secretion of large cargoes (53,55). In contrast to our studies, the prior report failed to use immunofluorescence to determine the degree to which TFG was depleted in cells, raising the distinct possibility that TFG was only partially reduced (47).…”

Section: Discussioncontrasting

confidence: 52%

“…Biochemical and genetic screens in human cells, Drosophila, and C. elegans have identified several factors that play important roles at the ER in cargo selection, exit site organization, and modulating secretory capacity, but components that facilitate movement of COPII-coated carriers between the ER and ERGIC have been more challenging to define (55,(64)(65)(66)(67). Microtubules and other cytoskeletal elements are absent within this region, but, nevertheless, most COPII-coated carriers cluster within the ER/ERGIC interface, suggesting the presence of an underlying meshwork that links the organelles to form an integrated secretory unit (44,68).…”

Section: Discussionmentioning

confidence: 99%

“…the actions of multiple regulators of COPII-mediated transport via its ability to associate with numerous factors including Sar1, Sec24, Sec31, Sec16, TRAPPC3, p125A, members of the TANGO1 cargo receptor family, and, now, TFG (10,14,36,39,(54)(55)(56). Some of these interactions have been shown to be competitive, suggesting that unique associations with Sec23 occur sequentially as transport carriers form, undergo scission from the ER, and tether to ERGIC membranes (14,40).…”

Section: Tfg Facilitates the Export Of Conventional Cargoes From The Ermentioning

confidence: 99%

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TFG facilitates outer coat disassembly on COPII transport carriers to promote tethering and fusion with ER–Golgi intermediate compartments

Hanna

Block

Frankel

et al. 2017

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

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The conserved coat protein complex II (COPII) mediates the initial steps of secretory protein trafficking by assembling onto subdomains of the endoplasmic reticulum (ER) in two layers to generate cargo-laden transport carriers that ultimately fuse with an adjacent ER–Golgi intermediate compartment (ERGIC). Here, we demonstrate that Trk-fused gene (TFG) binds directly to the inner layer of the COPII coat. Specifically, the TFG C terminus interacts with Sec23 through a shared interface with the outer COPII coat and the cargo receptor Tango1/cTAGE5. Our findings indicate that TFG binding to Sec23 outcompetes these other associations in a concentration-dependent manner and ultimately promotes outer coat dissociation. Additionally, we demonstrate that TFG tethers vesicles harboring the inner COPII coat, which contributes to their clustering between the ER and ERGIC in cells. Together, our studies define a mechanism by which COPII transport carriers are retained locally at the ER/ERGIC interface after outer coat disassembly, which is a prerequisite for fusion with ERGIC membranes.

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Section: Discussioncontrasting

confidence: 52%

Section: Discussionmentioning

confidence: 99%

Section: Tfg Facilitates the Export Of Conventional Cargoes From The Ermentioning

confidence: 99%

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TFG facilitates outer coat disassembly on COPII transport carriers to promote tethering and fusion with ER–Golgi intermediate compartments

Hanna

Block

Frankel

et al. 2017

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

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“…The role of Cideb in regulating SREBP/SCAP cargo loading may be analogous to other factors, such as TANGO1 and Sedlin, which have been shown to load unique cargos like pro‐collagen to specialized COPII transport vesicles for their ER export (Saito et al , ; Venditti et al , ; Liu et al , ). It is particularly noteworthy that unlike TANGO1 and Sedlin, Cideb may be part of the COPII vesicles.…”

Section: Discussionmentioning

confidence: 99%

Cideb controls sterol‐regulated ER export of SREBP / SCAP by promoting cargo loading at ER exit sites

Zhou

Chen

et al. 2019

The EMBO Journal

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SREBP s are master regulators of lipid homeostasis and undergo sterol‐regulated export from ER to Golgi apparatus for processing and activation via COPII ‐coated vesicles. While COPII recognizes SREBP through its escort protein SCAP , factor(s) specifically promoting SREBP / SCAP loading to the COPII machinery remains unknown. Here, we show that the ER /lipid droplet‐associated protein Cideb selectively promotes the loading of SREBP / SCAP into COPII vesicles. Sterol deprivation releases SCAP from Insig and enhances ER export of SREBP / SCAP by inducing SCAP ‐Cideb interaction, thereby modulating sterol sensitivity. Moreover, Cideb binds to the guanine nucleotide exchange factor Sec12 to enrich SCAP / SREBP at ER exit sites, where assembling of COPII complex initiates. Loss of Cideb inhibits the cargo loading of SREBP / SCAP , reduces SREBP activation, and alleviates diet‐induced hepatic steatosis. Our data point to a linchpin role of Cideb in regulated ER export of SREBP and lipid homeostasis.

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“…In this scenario, Tango1 functions as a critical receptor for collagen export, via its interaction with the collagen‐specific chaperone Hsp47, but does not regulate carrier size. However, a more general role for Tango and cTage5 must also be considered, given their constitutive presence at sites of COPII carrier formation . Recent evidence points to a potential role for Tango1 in the direct regulation of Sec16 distribution and function .…”

Section: Introductionmentioning

confidence: 99%

Membrane Transport at an Organelle Interface in the Early Secretory Pathway: Take Your Coat Off and Stay a While

et al. 2018

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Most metazoan organisms have evolved a mildly acidified and calcium diminished sorting hub in the early secretory pathway commonly referred to as the Endoplasmic Reticulum-Golgi intermediate compartment (ERGIC). These membranous vesicular-tubular clusters are found tightly juxtaposed to ER subdomains that are competent for the production of COPII-coated transport carriers. In contrast to many unicellular systems, metazoan COPII carriers largely transit just a few hundred nanometers to the ERGIC, prior to COPI-dependent transport on to the cis-Golgi. The mechanisms underlying formation and maintenance of ERGIC membranes are poorly defined. However, recent evidence suggests an important role for Trk-fused gene (TFG) in regulating the integrity of the ER/ERGIC interface. Moreover, in the absence of cytoskeletal elements to scaffold tracks on which COPII carriers might move, TFG appears to promote anterograde cargo transport by locally tethering COPII carriers adjacent to ERGIC membranes. This action, regulated in part by the intrinsically disordered domain of TFG, provides sufficient time for COPII coat disassembly prior to heterotypic membrane fusion and cargo delivery to the ERGIC.

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Tango1 spatially organizes ER exit sites to control ER export

Cited by 80 publications

References 67 publications

TFG facilitates outer coat disassembly on COPII transport carriers to promote tethering and fusion with ER–Golgi intermediate compartments

TFG facilitates outer coat disassembly on COPII transport carriers to promote tethering and fusion with ER–Golgi intermediate compartments

Cideb controls sterol‐regulated ER export of SREBP / SCAP by promoting cargo loading at ER exit sites

Membrane Transport at an Organelle Interface in the Early Secretory Pathway: Take Your Coat Off and Stay a While

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