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Cited by 226Cellular transport and secretionEndoplasmic Reticulum Stress and DiseaseHeat shock proteins research

Retrograde transport of Golgi-localized proteins to the ER

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Cole, Nelson B., Ellenberg, Jan, Song, Jia, DiEuliis, Diane, Lippincott-Schwartz, Jennifer·1998·The Journal of Cell Biology
DOI 10.1083/jcb.140.1.1PMC PMC2132605
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Abstract

The ER is uniquely enriched in chaperones and folding enzymes that facilitate folding and unfolding reactions and ensure that only correctly folded and assembled proteins leave this compartment. Here we address the extent to which proteins that leave the ER and localize to distal sites in the secretory pathway are able to return to the ER folding environment during their lifetime. Retrieval of proteins back to the ER was studied using an assay based on the capacity of the ER to retain misfolded proteins. The lumenal domain of the temperature-sensitive viral glycoprotein VSVGtsO45 was fused to Golgi or plasma membrane targeting domains. At the nonpermissive temperature, newly synthesized fusion proteins misfolded and were retained in the ER, indicating the VSVGtsO45 ectodomain was sufficient for their retention within the ER. At the permissive temperature, the fusion proteins were correctly delivered to the Golgi complex or plasma membrane, indicating the lumenal epitope of VSVGtsO45 also did not interfere with proper targeting of these molecules. Strikingly, Golgi-localized fusion proteins, but not VSVGtsO45 itself, were found to redistribute back to the ER upon a shift to the nonpermissive temperature, where they misfolded and were retained. This occurred over a time period of 15 min-2 h depending on the chimera, and did not require new protein synthesis. Significantly, recycling did not appear to be induced by misfolding of the chimeras within the Golgi complex. This suggested these proteins normally cycle between the Golgi and ER, and while passing through the ER at 40 degrees C become misfolded and retained. The attachment of the thermosensitive VSVGtsO45 lumenal domain to proteins promises to be a useful tool for studying the molecular mechanisms and specificity of retrograde traffic to the ER.

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  • Inhibition of the vacuolar-type H+-ATPase by concanamycin blocks the plus-end-directed transport of Golgi enzymes into the peripheral ER.

    “In support of such a hypothesis, inhibition of the vacuolar-type H+-ATPase by concanamycin blocks the plus-end–directed transport of Golgi enzymes into the peripheral ER (Cole et al., 1998).”

    From Light Chain– dependent Regulation of Kinesin's Interaction with Microtubules (1998) · cites this paper as Cole et al., 1998

    The Results section (Kinetics and Properties of Retrograde Transport; page not provided) reports that concanamycin B, a vacuolar proton-ATPase inhibitor, prevented a Golgi-localized VSVG–TGN38 fusion protein from redistributing into the ER. It does not establish that the blocked transport was plus-end-directed or demonstrate that concanamycin blocked transport of Golgi enzymes specifically into the peripheral ER. (LLM, conf=0.88)

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Authors
Cole, N. B., Ellenberg, J., Song, J., DiEuliis, D., & Lippincott-Schwartz, J.
Affiliations
  • National Institutes of Health (US)
  • *Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development; and ‡National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, Maryland 20892
ORCID
Venue
The Journal of Cell Biology
Publisher
Rockefeller University Press
Published
1998-01-12
Volume
140
Issue
1
Pages
1-15
ISSN
  • 0021-9525 (ISSN-L)
  • 1540-8140
DOI
10.1083/jcb.140.1.1
PMC
PMC2132605
OpenAlex
W2113736802
Cited by
226
References
78
Citations by year
2026: 1 · 2025: 3 · 2023: 3 · 2022: 3 · 2021: 4 · 2020: 3 · 2019: 6 · 2018: 1 · 2017: 1 · 2016: 3 · 2015: 6 · 2014: 5 · 2013: 6 · 2012: 2
FWCI
11.34
Type
journal article
Language
en
Open access
Licence
cc-by-nc-sa
Locations
  • The Journal of Cell Biology (publishedVersion)
  • Europe PMC (PubMed Central) (publishedVersion, cc-by-nc-sa)
  • PubMed Central (publishedVersion, cc-by-nc-sa)
  • PubMed (publishedVersion)
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 › Heat shock proteins research
Keywords
retrograde transport, endoplasmic reticulum retention, protein misfolding, protein recycling, secretory pathway, protein folding, fusion protein, lumenal domain
MeSH terms
Animals, Cell Membrane, Cycloheximide, Endoplasmic Reticulum, Golgi Apparatus, Cricetinae, Membrane Glycoproteins, Models, Molecular, Protein Conformation, Recombinant Fusion Proteins, Simian virus 40, Temperature, Transfection, Viral Envelope Proteins, Mutagenesis, Site-Directed, CHO Cells, Protein Folding, Receptors, Peptide, COS Cells

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