The structure of the COPII transport-vesicle coat assembled on membranes

Zanetti, Giulia; Prinz, Simone; Daum, Sebastian; Meister, Annette; Schekman, Randy; Bacia, Kirsten; Briggs, John

doi:10.7554/elife.00951

Cited by 124 publications

(169 citation statements)

References 35 publications

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“…(C) All-atom representation of the Sec23a/24d crystal structure with bound TANGO PPP peptide (peptide sequence GPRPLPPP) (Table S1) bilayer surface (estimated from the tomography images presented in ref. 17).…”

Section: Discussionmentioning

confidence: 99%

“…Structural studies have established that the adaptability of the COPII coat (i.e., the capacity to adopt vesicular and tubular forms) depends on two molecular features: variable angles at the vertex, and centrally along the edge, of the Sec13/31 cage; and a flexible (unstructured) polypeptide connection between the inner and outer coat proteins (17,22,25). The variable angles enable the Sec13/31 assembly unit to adapt to cages of different curvature (in two dimensions), and the flexible link between Sec23/24•Sar1 and Sec13/31 allows for variation in the geometric relationship between the inner and outer coat proteins (17).…”

Section: Discussionmentioning

confidence: 99%

“…COPII-coated tubules are observed as straight-sided tubes (17), or with a beads-ona-string appearance in which regular constrictions may arise from aborted attempts at membrane fission (14,16). Whereas vesicles contain a Sec23/24 inner coat and a self-assembled Sec13/31 cage with isometric (cubic) symmetry, tubules are coated with a distinctive, close-packed Sec23/24 helical lattice and a rhomboidal Sec13/31 cage (17). The realization that COPII coat proteins can form two distinct and mutually incompatible lattices suggests the hypothesis that COPII carrier formation involves two self-assembly reactions that compete to determine the shape of the COPII carrier-either the isometric small vesicle or the helical tubulewith the outcome of budding influenced by regulatory proteins that promote one or other lattice.…”

mentioning

confidence: 99%

“…Important in this respect is the observation of tubular COPII carriers with dimensions commensurate with procollagen cargo; such tubules form, along with small vesicles, in budding reactions in vivo and in vitro (14)(15)(16). COPII-coated tubules are observed as straight-sided tubes (17), or with a beads-ona-string appearance in which regular constrictions may arise from aborted attempts at membrane fission (14,16). Whereas vesicles contain a Sec23/24 inner coat and a self-assembled Sec13/31 cage with isometric (cubic) symmetry, tubules are coated with a distinctive, close-packed Sec23/24 helical lattice and a rhomboidal Sec13/31 cage (17).…”

mentioning

confidence: 99%

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TANGO1/cTAGE5 receptor as a polyvalent template for assembly of large COPII coats

Goldberg

2016

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

102

159

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The supramolecular cargo procollagen is loaded into coat protein complex II (COPII)-coated carriers at endoplasmic reticulum (ER) exit sites by the receptor molecule TANGO1/cTAGE5. Electron microscopy studies have identified a tubular carrier of suitable dimensions that is molded by a distinctive helical array of the COPII inner coat protein Sec23/24•Sar1; the helical arrangement is absent from canonical COPII-coated small vesicles. In this study, we combined X-ray crystallographic and biochemical analysis to characterize the association of TANGO1/cTAGE5 with COPII proteins. The affinity for Sec23 is concentrated in the proline-rich domains (PRDs) of TANGO1 and cTAGE5, but Sec23 recognizes merely a PPP motif. The PRDs contain repeated PPP motifs separated by proline-rich linkers, so a single TANGO1/cTAGE5 receptor can bind multiple copies of coat protein in a close-packed array. We propose that TANGO1/cTAGE5 promotes the accretion of inner coat proteins to the helical lattice. Furthermore, we show that PPP motifs in the outer coat protein Sec31 also bind to Sec23, suggesting that stepwise COPII coat assembly will ultimately displace TANGO1/cTAGE5 and compartmentalize its operation to the base of the growing COPII tubule.vesicle traffic | coat protein | procollagen T he coat protein complex II (COPII)-coated vesicles transport secretory and plasma membrane proteins from the endoplasmic reticulum (ER). COPII vesicle budding involves a stepwise assembly reaction: Membrane-bound Sar1-GTP recruits Sec23/24 to form the inner coat complex that, in turn, recruits the Sec13/31 outer coat protein (1). Sec13/31 self-assembles into a polyhedron, and in the process, it sculpts the ER membrane into a bud, producing a COPII-coated vesicle with a diameter of ∼60 nm (2-4).Small cargo molecules are captured during the budding reaction through mechanisms that are well established (5). However, the formation of canonical 60-nm COPII vesicles cannot explain the packaging of large cargos, such as the procollagen fibril with a length of 300-400 nm. Procollagen follows the conventional route of secretion taken by other extracellular proteins, and its ER export evidently depends on COPII carriers because mutations in genes encoding COPII proteins result in collagen secretion blockade, impaired extracellular matrix deposition, and abnormal craniofacial development (6-8). A key discovery was the identification of the receptor TANGO1 and its coreceptor cTAGE5 as ER-localized machinery for loading procollagen into COPII carriers (9, 10). TANGO1 has a luminal SH3 domain shown to interact with collagen VII and a cytosolic domain that interacts with Sec23/24. Both TANGO1 and cTAGE5 are required for collagen export from the ER (9, 10). The TANGO1 knockout mouse has generalized defects in extracellular matrix formation, owing to a block in ER export of multiple collagen types (11).Recent research has implicated post-ER membranes in TANGO1-mediated carrier formation (12, 13); however, the mechanism of action of TANGO1/cTAGE5 in procollagen export...

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

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TANGO1/cTAGE5 receptor as a polyvalent template for assembly of large COPII coats

Goldberg

2016

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

102

159

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“…Nous disposons maintenant d'explications détaillées du mécanisme de polymérisation des deux feuillets du manteau et d'un aperçu critique de l'échafaudage complexe qui forme le feuillet externe : un treillis polyédrique régulier que Balch a découvert dans une réaction d'auto-assemblage avec l'hétérotétramère mammalien purifié Sec13/31. Une ancienne collaboratrice post-doc, Giulia Zanetti, a récemment visualisé en microscopie cryoélectronique le réseau de COPII en treillis forméà la surface d'un liposome synthétique (Zanetti et al, 2013). Malgré le peu d'indications qui suggèrent des différences fonctionnelles ou structurales entre les protéines COPII des mammifères et celles de la levure, les mammifères ont la capacité de réguler la taille du manteau pour contenir des complexes de grande taille ou de forme irrégulière, comme les lipoprotéines et le pro-collagène.…”

Section: Copii Est Responsable Du Bourgeonnement Vésiculaireà Partirunclassified

Les gènes et les protéines qui contrôlent la voie de sécrétion

Schekman

2015

Biologie Aujourd'hui

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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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The structure of the COPII transport-vesicle coat assembled on membranes

Cited by 124 publications

References 35 publications

TANGO1/cTAGE5 receptor as a polyvalent template for assembly of large COPII coats

TANGO1/cTAGE5 receptor as a polyvalent template for assembly of large COPII coats

Les gènes et les protéines qui contrôlent la voie de sécrétion

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

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