title: TANGO1 assembles into rings around COPII coats at ER exit sites.
abstract: TANGO1 (transport and Golgi organization 1) interacts with CTAGE5 and COPII components Sec23/Sec24 and recruits ERGIC-53 (endoplasmic reticulum [ER]-Golgi intermediate compartment 53)-containing membranes to generate a mega-transport carrier for export of collagens and apolipoproteins from the ER. We now show that TANGO1, at the ER, assembles in a ring that encircles COPII components. The C-terminal, proline-rich domains of TANGO1 molecules in the ring are initially tilted onto COPII coats but appear to be pushed apart as the carrier grows. These findings lend support to our suggestion that growth of transport carriers for exporting bulky cargoes requires addition of membranes and not simply COPII-mediated accretion of a larger surface of ER. TANGO1 remains at the neck of the newly forming transport carrier, which grows in size by addition of ERGIC-53-containing membranes to generate a transport intermediate for the export of bulky collagens.
authors.affiliation: Centre for Genomic Regulation (CRG), The Barcelona Institute of Science and Technology, 08003 Barcelona, Spain.|Universitat Pompeu Fabra (UPF), 08002 Barcelona, Spain.
authors.forename: Ishier
authors.identifier: 0000-0002-5898-4896
authors.initials: I
authors.lastname: Raote
authors.affiliation: Centre for Genomic Regulation (CRG), The Barcelona Institute of Science and Technology, 08003 Barcelona, Spain.|Universitat Pompeu Fabra (UPF), 08002 Barcelona, Spain.
authors.forename: Maria
authors.identifier: 0000-0003-0845-2610
authors.initials: M
authors.lastname: Ortega Bellido
authors.affiliation: Institute of Protein Biochemistry, 80131 Naples, Italy.
authors.forename: Marinella
authors.initials: M
authors.lastname: Pirozzi
authors.affiliation: SIMBIOsys Group, Department of Information and Communication Technologies, Universitat Pompeu Fabra (UPF), 08018 Barcelona, Spain.
authors.forename: Chong
authors.initials: C
authors.lastname: Zhang
authors.affiliation: Department of Molecular and Cellular Biology, Howard Hughes Medical Institute, University of California, Berkeley, Berkeley, CA 94720.
authors.forename: David
authors.initials: D
authors.lastname: Melville
authors.affiliation: Institute of Protein Biochemistry, 80131 Naples, Italy.
authors.forename: Seetharaman
authors.initials: S
authors.lastname: Parashuraman
authors.affiliation: Centre for Genomic Regulation (CRG), The Barcelona Institute of Science and Technology, 08003 Barcelona, Spain.|Universitat Pompeu Fabra (UPF), 08002 Barcelona, Spain.|Advanced Light Microscopy Unit, Centre for Genomic Regulation (CRG), 08003 Barcelona, Spain.
authors.forename: Timo
authors.initials: T
authors.lastname: Zimmermann
authors.affiliation: Centre for Genomic Regulation (CRG), The Barcelona Institute of Science and Technology, 08003 Barcelona, Spain vivek.malhotra@crg.eu.|Universitat Pompeu Fabra (UPF), 08002 Barcelona, Spain.|Institució Catalana de Recerca i Estudis Avançats (ICREA), 08010 Barcelona, Spain.
authors.forename: Vivek
authors.identifier: 0000-0001-6198-7943
authors.initials: V
authors.lastname: Malhotra
mesh_terms: D051784:Aryl Hydrocarbon Receptor Nuclear Translocator / Q000378:metabolism*; D022181:COP-Coated Vesicles / Q000378:metabolism*; D018938:Caco-2 Cells; D045744:Cell Line, Tumor; D004721:Endoplasmic Reticulum / Q000378:metabolism*; D006056:Golgi Apparatus / Q000378:metabolism; D006367:HeLa Cells; D006801:Humans; D008565:Membrane Proteins / Q000378:metabolism; D021381:Protein Transport / Q000502:physiology; D033921:Vesicular Transport Proteins / Q000378:metabolism
chemical_list: D008565:Membrane Proteins; D033921:Vesicular Transport Proteins; D051784:Aryl Hydrocarbon Receptor Nuclear Translocator