Cited by 102Cellular transport and secretionAutophagy in Disease and TherapyCalcium signaling and nucleotide metabolism

Segregation in the Golgi complex precedes export of endolysosomal proteins in distinct transport carriers

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Chen, Yu, Gershlick, David C., Park, Sang Yoon, Bonifacino, Juan S.·2017·Journal of Cell Biology

Abstract

Biosynthetic sorting of newly synthesized transmembrane cargos to endosomes and lysosomes is thought to occur at the TGN through recognition of sorting signals in the cytosolic tails of the cargos by adaptor proteins, leading to cargo packaging into coated vesicles destined for the endolysosomal system. Here we present evidence for a different mechanism in which two sets of endolysosomal proteins undergo early segregation to distinct domains of the Golgi complex by virtue of the proteins’ luminal and transmembrane domains. Proteins in one Golgi domain exit into predominantly vesicular carriers by interaction of sorting signals with adaptor proteins, but proteins in the other domain exit into predominantly tubular carriers shared with plasma membrane proteins, independently of signal–adaptor interactions. These findings demonstrate that sorting of endolysosomal proteins begins at an earlier stage and involves mechanisms that partly differ from those described by classical models.

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  • TfR is loaded into tubular carriers derived from the TGN in nonpolarized HeLa cells by an AP-1-independent process.

    “which showed that TfR is loaded into tubular carriers derived from the TGN in nonpolarized HeLa cells by an AP-1–independent process (Chen et al., 2017).”

    From Distinct anterograde trafficking pathways of BACE1 and amyloid precursor protein from the TGN and the regulation of amyloid-β production (2020) · cites this paper as Chen et al., 2017

    The Results section ('Exit of LAMP1 and TfR in tubular carriers is independent of signal–adaptor interactions'; page unavailable) reports TfR incorporation into Golgi-derived tubular carriers in HeLa cells and says AP-complex knockout did not affect its exit in those carriers. The Discussion ('Molecular determinants of early Golgi segregation and Golgi export'; page unavailable) explicitly says this exit is AP-1-independent. The paper describes the carriers as Golgi-derived, but the cited passages do not establish the more specific claim that they originate from the TGN. (LLM, conf=0.82)

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Sorted by citations

Authors
Chen, Y., Gershlick, D. C., Park, S. Y., & Bonifacino, J. S.
Affiliations
  • National Institutes of Health (US)
  • Cell Biology and Neurobiology Branch, Eunice Kennedy Shriver National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD
Corresponding author
Bonifacino, Juan S.
Venue
Journal of Cell Biology
Published
2017-10-04
Volume
216
Issue
12
Pages
4141-4151
ISSN
  • 0021-9525 (ISSN-L)
  • 1540-8140
OpenAlex
W2760834034
Cited by
102
References
0
Citations by year
2026: 7 · 2025: 13 · 2024: 14 · 2023: 9 · 2022: 14 · 2021: 8 · 2020: 14 · 2019: 19 · 2018: 3 · 2017: 1
FWCI
5.27
Type
journal article
Language
en
Open access
Locations
  • The Journal of Cell Biology (publishedVersion, cc-by-nc-sa)
  • Europe PMC (PubMed Central) (publishedVersion, cc-by-nc-sa)
  • PubMed Central (publishedVersion, cc-by-nc-sa)
  • PubMed (publishedVersion)
Funders
  • National Institute of Child Health and Human Development
  • National Institutes of Health (ZIA HD001607)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
  • Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Physiology › Calcium signaling and nucleotide metabolism
Keywords
Golgi apparatus, protein sorting, trans-Golgi network, adaptor proteins, sorting signals, lysosomal biogenesis, endosomes, plasma membrane proteins
MeSH terms
Amino Acid Sequence, HeLa Cells, Humans, Lysosomes, Receptors, Transferrin, Endosomes, Antigens, CD, Gene Expression, Receptor, IGF Type 2, Protein Transport, Protein Sorting Signals, trans-Golgi Network, Adaptor Protein Complex 2, Lysosomal Membrane Proteins, Lysosomal-Associated Membrane Protein 1, CRISPR-Cas Systems

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