Skip to main navigation Skip to search Skip to main content

The em structure of the TRAPPIII complex leads to the identification of a requirement for COPII vesicles on the macroautophagy pathway

  • Dongyan Tan
  • , Yiying Cai
  • , Juan Wang
  • , Jinzhong Zhang
  • , Shekar Menon
  • , Hui Ting Chou
  • , Susan Ferro-Novick
  • , Karin M. Reinisch
  • , Thomas Walz
  • Yale University
  • University of California at San Diego
  • Affymetric, Inc.
  • Harvard University
  • Howard Hughes Medical Institute

Research output: Contribution to journalArticlepeer-review

126 Scopus citations

Abstract

The transport protein particle (TRAPP) III complex, comprising the TRAPPI complex and additional subunit Trs85, is an autophagyspecific guanine nucleotide exchange factor for the Rab GTPase Ypt1 that is recruited to the phagophore assembly site when macroautophagy is induced. We present the single-particle electron microscopy structure of TRAPPIII, which reveals that the domeshaped Trs85 subunit associates primarily with the Trs20 subunit of TRAPPI. We further demonstrate that TRAPPIII binds the coat protein complex (COP) II coat subunit Sec23. The COPII coat facilitates the budding and targeting of ER-derived vesicles with their acceptor compartment. We provide evidence that COPII-coated vesicles and the ER-Golgi fusion machinery are needed for macroautophagy. Our results imply that TRAPPIII binds to COPII vesicles at the phagophore assembly site and that COPII vesicles may provide one of the membrane sources used in autophagosome formation. These events are conserved in yeast to mammals.

Original languageEnglish
Pages (from-to)19432-19437
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Volume110
Issue number48
DOIs
StatePublished - Nov 26 2013

Fingerprint

Dive into the research topics of 'The em structure of the TRAPPIII complex leads to the identification of a requirement for COPII vesicles on the macroautophagy pathway'. Together they form a unique fingerprint.

Cite this