Cited by 108Cellular transport and secretionEndoplasmic Reticulum Stress and DiseaseExtracellular vesicles in disease

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

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Ma, Wenfu, Goldberg, Jonathan·2016·Proceedings of the National Academy of Sciences

DOI 10.1073/pnas.1605916113PMC PMC5018777

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Abstract

Significance: Proteins destined for secretion from cells enter the secretory pathway in coat protein complex II (COPII)-coated vesicles budding from the endoplasmic reticulum (ER). Most cargo proteins are small and exit the ER in 60-nm vesicles. However, some secretory cargos are too large to enter such carriers; in particular, the procollagen precursor of the extracellular matrix exits the ER as a 300- to 400-nm fibril. Recent research suggests that procollagen may be packaged into large COPII-coated tubules, guided by the receptor molecule TANGO1/cTAGE5. We show that each TANGO1/cTAGE5 receptor protein has a multiplicity of binding sites to recruit and concentrate COPII proteins. We propose the model that TANGO1/cTAGE5 instructs the COPII coat to form large tubular carriers.

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Authors: Ma, W., & Goldberg, J.
Affiliations: Memorial Sloan Kettering Cancer Center (US)
Corresponding author: Goldberg, Jonathan
ORCID: Ma, Wenfu
Goldberg, Jonathan
Venue: Proceedings of the National Academy of Sciences
Publisher: National Academy of Sciences
Published: 2016-08-22
Volume: 113
Issue: 36
Pages: 10061-10066
ISSN: 0027-8424 (ISSN-L)
1091-6490
DOI: 10.1073/pnas.1605916113
PMC: PMC5018777
OpenAlex: W2517050669
Cited by: 108
References: 36
Citations by year: 2026: 7 · 2025: 11 · 2024: 12 · 2023: 9 · 2022: 10 · 2021: 17 · 2020: 8 · 2019: 11 · 2018: 15 · 2017: 7 · 2016: 1
FWCI: 7.81
Type: journal article
Language: en
Open access: bronze
doi.org
Locations: Proceedings of the National Academy of Sciences (publishedVersion)
Europe PMC (PubMed Central) (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
OSTI OAI (U.S. Department of Energy Office of Scientific and Technical Information) (submittedVersion)
Funders: Memorial Sloan-Kettering Cancer Center (CA008748, P30 CA008748)
National Cancer Institute (P30CA008748)
Argonne National Laboratory
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Endoplasmic Reticulum Stress and Disease
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Extracellular vesicles in disease
Keywords: TANGO1, Sec23, Sec31, Sar1, proline-rich region, ER exit sites, coated vesicles, protein-protein interaction
MeSH terms: Protein Conformation, alpha-Helical, Protein Conformation, beta-Strand, Antigens, Neoplasm, Binding Sites, Endoplasmic Reticulum, Humans, Models, Molecular, Neoplasm Proteins, Procollagen, Protein Binding, Recombinant Proteins, Gene Expression, Crystallography, X-Ray, Monomeric GTP-Binding Proteins, Amino Acid Motifs, Protein Transport, COP-Coated Vesicles, Vesicular Transport Proteins, Aryl Hydrocarbon Receptor Nuclear Translocator, Protein Interaction Domains and Motifs

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

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