CoChat
Sign Up
Cited by 652

The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.

Hrs sorts ubiquitinated proteins into clathrin-coated microdomains of early endosomes

Raiborg, Camilla, Bache, Kristi G., Gillooly, David J., Madshus, Inger Helene, Stang, Espen, Stenmark, Harald·2002·Nature Cell Biology
DOI 10.1038/ncb791
Open this paper in CoChat — free account

Abstract

After endocytosis, some membrane proteins recycle from early endosomes to the plasma membrane whereas others are transported to late endosomes and lysosomes for degradation. Conjugation with the small polypeptide ubiquitin is a signal for lysosomal sorting. Here we show that the hepatocyte growth factor-regulated tyrosine kinase substrate, Hrs, is involved in the endosomal sorting of ubiquitinated membrane proteins. Hrs contains a clathrin-binding domain, and by electron microscopy we show that Hrs localizes to flat clathrin lattices on early endosomes. We demonstrate that Hrs binds directly to ubiquitin by way of a ubiquitin-interacting motif (UIM), and that ubiquitinated proteins localize specifically to Hrs- and clathrin-containing microdomains. Whereas endocytosed transferrin receptors fail to colocalize with Hrs and rapidly recycle to the cell surface, transferrin receptors that are fused to ubiquitin interact with Hrs, localize to Hrs- and clathrin-containing microdomains and are sorted to the degradative pathway. Overexpression of Hrs strongly and specifically inhibits recycling of ubiquitinated transferrin receptors by a mechanism that requires a functional UIM. We conclude that Hrs sorts ubiquitinated membrane proteins into clathrin-coated microdomains of early endosomes, thereby preventing their recycling to the cell surface.

Overview

Integrity signals

Registry

Crossref · 10.1038/ncb791

Cites

1 of 1 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Verification

Claims the paper makes

This paper’s full text isn’t openly available, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

  • The ESCRT-0 complex partitions cargo arriving at the sorting endosome between recycling and progression to the MVB.

    “The ESCRT-0 complex, consisting of adaptor proteins hepatocyte growth factor-regulated substrate (Hrs) and signal transducing adaptor molecule (STAM) (9), partitions cargo arriving at the sorting endosome between recycling and progression to the MVB (10 -13)”

    From Regulation of Epidermal Growth Factor Receptor Ubiquitination and Trafficking by the USP8·STAM Complex (2010) · cites this paper as [12]

  • HRS binds directly to ubiquitinated proteins, which are then sorted to clathrin-coated microdomains while nonubiquitinated receptors, like transferrin or LDL receptor, are rapidly recycled to the cell surface.

    “HRS binds directly to ubiquitinated proteins, which are then sorted to clathrin-coated microdomains while nonubiquitinated receptors, like transferrin or LDL receptor, are rapidly recycled to the cell surface (45).”

    From Essential Role of Ubiquitin-Specific Protease 8 for Receptor Tyrosine Kinase Stability and Endocytic Trafficking In Vivo (2007) · cites this paper as [45]

Citations

Cites

Flagged first, then by citations

Research works printed but not linked: 29

  1. Gruenberg, J. Nature Rev. Mol. Cell Biol. 2, 721–730 (2001). · DOI
  2. Hicke, L. Nature Rev. Mol. Cell Biol. 2, 195–201 (2001). · DOI
  3. Dupre, S., Volland, C. & Haguenauer-Tsapis, R. Curr. Biol. 11, R932–R934 (2001). · DOI
  4. Komada, M. & Kitamura, N. Mol. Cell Biol. 15, 6213–6221 (1995). · DOI · Paper page
  5. Raiborg, C., Bache, K. G., Mehlum, A., Stang, E. & Stenmark, H. EMBO J. 20, 5008–5021 (2001). · DOI
  6. Stoorvogel, W., Oorschot, V. & Geuze, H. J. J. Cell Biol. 132, 21–33 (1996). · DOI
  7. Hofmann, K. & Falquet, L. Trends Biochem. Sci. 26, 347–350 (2001). · DOI
  8. Lloyd, T. E. et al. Cell 108, 261–269 (2002). · DOI · Paper page
  9. Stenmark, H. et al. EMBO J. 13, 1287–1296 (1994). · DOI · Paper page
  10. Hopkins, C. R. Cell 35, 321–330 (1983). · DOI
  11. Brodsky, F. M., Chen, C. Y., Knuehl, C., Towler, M. C. & Wakeham, D. E. Annu. Rev. Cell Dev. Biol. 17, 517–568 (2001). · DOI
  12. Hirst, J. & Robinson, M. S. Biochim. Biophys. Acta 1404, 173–193 (1998). · DOI
  13. Levkowitz, G. et al. Mol. Cell 4, 1029–1040 (1999). · DOI
  14. Shenoy, S. K., McDonald, P. H., Kohout, T. A. & Lefkowitz, R. J. Science 294, 1307–1313 (2001). · DOI
  15. Rocca, A., Lamaze, C., Subtil, A. & Dautry-Varsat, A. Mol. Biol. Cell 12, 1293–1301 (2001). · DOI
  16. Reggiori, F. & Pelham, H. R. EMBO J. 20, 5176–5186 (2001). · DOI · Paper page
  17. Urbanowski, J. L. & Piper, R. C. Traffic. 2, 622–630 (2001). · DOI
  18. Van Kerkhof, P., Govers, R., Alves dos Santos, C. M. & Strous, G. J. J. Biol. Chem. 275, 1575–1580 (2000). · DOI
  19. Asao, H. et al. J. Biol. Chem. 272, 32785–32791 (1997). · DOI
  20. Takata, H., Kato, M., Denda, K. & Kitamura, N. Genes Cells 5, 57–69 (2000). · DOI · Paper page
  21. Bean, A. J. et al. J. Biol. Chem. 275, 15271–15278 (2000). · DOI
  22. Katzmann, D. J., Babst, M. & Emr, S. D. Cell 106, 145–155 (2001). · DOI
  23. Evan, G. I., Lewis, G. K., Ramsay, G. & Bishop, J. M. Mol. Cell Biol. 5, 3610–3616 (1985). · DOI
  24. Mu, F. T. et al. J. Biol. Chem. 270, 13503–13511 (1995). · DOI
  25. Zerial, M., Melancon, P., Schneider, C. & Garoff, H. EMBO J. 5, 1543–1550 (1986). · DOI
  26. Vojtek, A. B., Hollenberg, S. M. & Cooper, J. A. Cell 74, 205–214 (1993). · DOI
  27. Griffiths, G., McDowall, A., Back, R. & Dubochet, J. J. Ultrastruct. Res. 89, 65–78 (1984). · DOI
  28. Sutter, G., Ohlmann, M. & Erfle, V. FEBS Lett. 371, 9–12 (1995). · DOI
  29. Simonsen, A., Bremnes, B., Rønning, E., Aasland, R. & Stenmark, H. Eur. J. Cell Biol. 75, 223–231 (1998). · DOI

Cited by

Sorted by citations

Metadata

Authors
Raiborg, C., Bache, K. G., Gillooly, D. J., Madshus, I. H., Stang, E., & Stenmark, H.
Venue
Nature Cell Biology
Publisher
Springer Science and Business Media LLC
Published
2002-04-29
Volume
4
Issue
5
Pages
394-398
ISSN
  • 1465-7392
  • 1476-4679
DOI
10.1038/ncb791
Cited by
652
References
1
Language
en
Licence

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review