4.7 Article

TANGO1 assembles into rings around COP II coats at ER exit sites

Journal

JOURNAL OF CELL BIOLOGY
Volume 216, Issue 4, Pages 901-909

Publisher

ROCKEFELLER UNIV PRESS
DOI: 10.1083/jcb.201608080

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Funding

  1. Ministerio de Economia, Industria y Competitividad Plan Nacional [BFU2013-44188-P]
  2. Consolider [CSD2009-00016]
  3. Spanish Ministry of Economy and Competitiveness, through the Programmes Centro de Excelencia Severo Ochoa [SEV-2012-0208]
  4. Maria de Maeztu Units of Excellence in RD [MDM-2015-0502]
  5. European Union Seventh Framework Program (FP7) under European Research Council [268692]
  6. ICREA Funding Source: Custom

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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 COP II 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.

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