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


Authors: Ma, W.; Goldberg, J.
Article Title: TANGO1/cTAGE5 receptor as a polyvalent template for assembly of large COPII coats
Abstract: 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.
Keywords: procollagen; coat protein; vesicle traffic
Journal Title: Proceedings of the National Academy of Sciences of the United States of America
Volume: 113
Issue: 36
ISSN: 0027-8424
Publisher: National Academy of Sciences  
Date Published: 2016-09-06
Start Page: 10061
End Page: 10066
Language: English
DOI: 10.1073/pnas.1605916113
PROVIDER: scopus
PMCID: PMC5018777
PUBMED: 27551091
DOI/URL:
Notes: Conference Paper -- Export Date: 3 October 2016 -- Source: Scopus
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  1. Wenfu Ma
    4 Ma