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Bilayered Clathrin Coats on Endosomal Vacuoles Are Involved in Protein Sorting toward Lysosomes

Sachse, Martin, Urbé, Sylvie, Oorschot, Viola, Strous, Ger J., Klumperman, Judith·2002·Molecular Biology of the Cell
DOI 10.1091/mbc.01-10-0525
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Abstract

In many cells endosomal vacuoles show clathrin coats of which the function is unknown. Herein, we show that this coat is predominantly present on early endosomes and has a characteristic bilayered appearance in the electron microscope. By immunoelectron miscroscopy we show that the coat contains clathrin heavy as well as light chain, but lacks the adaptor complexes AP1, AP2, and AP3, by which it differs from clathrin coats on endocytic vesicles and recycling endosomes. The coat is insensitive to short incubations with brefeldin A, but disappears in the presence of the phosphatidylinositol 3-kinase inhibitor wortmannin. No association of endosomal coated areas with tracks of tubulin or actin was found. By quantitative immunoelectron microscopy, we found that the lysosomal-targeted receptors for growth hormone (GHR) and epidermal growth factor are concentrated in the coated membrane areas, whereas the recycling transferrin receptor is not. In addition, we found that the proteasomal inhibitor MG 132 induces a redistribution of a truncated GHR (GHR-369) toward recycling vesicles, which coincided with a redistribution of endosomal vacuole-associated GHR-369 to the noncoated areas of the limiting membrane. Together, these data suggest a role for the bilayered clathrin coat on vacuolar endosomes in targeting of proteins to lysosomes.

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  • Core retrieval and recycling complexes localise to specific retrieval sub-domains that are physically distinct from ESCRT-demarcated degradative sub-domains on the same endosome.

    “On the limiting membrane of endosomes, electron and light microscopy has established that core retrieval and recycling complexes localise to specific retrieval sub-domains that, while present on the same endosome, are physically distinct from ESCRT-demarcated degradative sub-domains19,32–37.”

    From Mapping of endosomal proximity proteomes reveals Retromer as a hub for RAB GTPase regulation (2025) · cites this paper as [32]

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Metadata

Authors
Sachse, M., Urbé, S., Oorschot, V., Strous, G. J., & Klumperman, J.
Affiliations
  • Department of Cell Biology, University Medical Center Utrecht and Institute of Biomembranes, 3584 CX Utrecht, The Netherlands;
  • Physiological Laboratory, University of Liverpool, Liverpool L69 3BX, United Kingdom
Venue
Molecular Biology of the Cell
Publisher
American Society for Cell Biology (ASCB)
Published
2002-04
Volume
13
Issue
4
Pages
1313-1328
ISSN
  • 1059-1524
  • 1939-4586
DOI
10.1091/mbc.01-10-0525
Cited by
321
References
1
Language
en

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