Cited by 35

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

Cargo induces retromer-mediated membrane remodeling on membranes

Purushothaman, Latha Kallur, Ungermann, Christian·2018·Molecular Biology of the Cell

Abstract

Endosomes serve as a central sorting station of lipids and proteins that arrive via vesicular carrier from the plasma membrane and the Golgi complex. At the endosome, retromer complexes sort selected receptors and membrane proteins into tubules or vesicles that bud off the endosome. The mature endosome finally fuses with the lysosome. Retromer complexes consist of a cargo selection complex (CSC) and a membrane remodeling part (sorting nexin [SNX]-Bin/amphiphysin/Rvs [BAR], or Snx3 in yeast) and different assemblies of retromer mediate recycling of different cargoes. Due to this complexity, the exact order of events that results in carrier formation is not yet understood. Here, we reconstituted this process on giant unilamellar vesicles together with purified retromer complexes from yeast and selected cargoes. Our data reveal that the membrane remodeling activity of both Snx3 and the SNX-BAR complex is strongly reduced at low concentrations, which can be reactivated by CSC. At even lower concentrations, these complexes still associate with membranes, but only remodel membranes in the presence of their specific cargoes. Our data thus favor a simple model, where cargo functions as a specific trigger of retromer-mediated sorting on endosomes.

Overview

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Integrity signals

Registry

Crossref · 10.1091/mbc.e18-06-0339

Cites

1 of 1 references verified0 citation errors · 0 not checkable

Statistics

Verification

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

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?

  • Various sorting nexin proteins, such as SNX27, SNX32, SNX1-SNX6, and SNX1-SNX5, are autoinhibited in the basal state, with cargo binding enhancing their association with Retromer or membranes.

    “Interestingly, various sorting nexin proteins, such as SNX2729, SNX326,39, SNX1-SNX628, and SNX1-SNX540, operate similarly, being autoinhibited in the basal state, with cargo binding enhancing their association with Retromer or membranes.”

    From Structural basis for Retriever-SNX17 assembly and endosomal sorting (2024) · cites this paper as [39]

    The Results (‘Cargo can be limiting for SNX-retromer membrane remodeling activity’; page unavailable) show that Vps10 cargo induces SNX-BAR retromer tubulation under conditions where it otherwise does not occur. The Discussion proposes that cargo may promote assembly of SNX-BAR and retromer complexes, but does not establish basal autoinhibition or the claimed mechanism across SNX27, SNX32, SNX1–SNX6, and SNX1–SNX5. (LLM, conf=0.86)

    Experimental — accuracy not yet measured

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Citations

Cites

Flagged first, then by citations

Research works printed but not linked: 41

  1. Antonny B, 2016, EMBO J, 35, 2270, 10.15252/embj.201694613 · DOI
  2. 10.1091/mbc.E14-08-1318 · DOI
  3. Arlt H, 2015, J Cell Sci, 128, 645, 10.1242/jcs.132720 · DOI
  4. Balderhaar HJK, 2010, J Cell Sci, 123, 4085, 10.1242/jcs.071977 · DOI
  5. Barr FA, 2013, J Cell Biol, 202, 191, 10.1083/jcb.201306010 · DOI
  6. Chi RJ, 2014, J Cell Biol, 202, 527
  7. Cullen PJ, 2008, Nat Rev Mol Cell Biol, 9, 574, 10.1038/nrm2427 · DOI · Paper page
  8. Daumke O, 2014, Cell, 156, 882, 10.1016/j.cell.2014.02.017 · DOI
  9. Frost A, 2009, Cell, 137, 191, 10.1016/j.cell.2009.04.010 · DOI · Paper page
  10. Gomez-Navarro N, 2016, Curr Biol, 26, R54, 10.1016/j.cub.2015.12.017 · DOI
  11. Goody RS, 2017, Biol Chem, 398, 565, 10.1515/hsz-2016-0274 · DOI
  12. Gopaldass N, 2017, EMBO J, 36, 3274, 10.15252/embj.201796859 · DOI · Paper page
  13. Harrison MS, 2014, Proc Natl Acad Sci, 111, 267, 10.1073/pnas.1316482111 · DOI
  14. Harterink M, 2011, Nat Cell Biol, 13, 914, 10.1038/ncb2281 · DOI · Paper page
  15. Heinrich R, 2005, J Cell Biol, 168, 271, 10.1083/jcb.200409087 · DOI
  16. Henne WM, 2011, Dev Cell, 21, 77, 10.1016/j.devcel.2011.05.015 · DOI
  17. Hettema E, 2003, EMBO J, 22, 548, 10.1093/emboj/cdg062 · DOI
  18. Huotari J, 2011, EMBO J, 30, 3481, 10.1038/emboj.2011.286 · DOI
  19. Janke C, 2004, Yeast, 21, 947, 10.1002/yea.1142 · DOI
  20. Jimenez-Orgaz A, 2018, EMBO J, 37, 235, 10.15252/embj.201797128 · DOI · Paper page
  21. Klumperman J, 2014, Cold Spring Harb Perspect Biol, 6, a016857, 10.1101/cshperspect.a016857 · DOI
  22. Kvainickas A, 2017, J Cell Biol, 216, 3677, 10.1083/jcb.201702137 · DOI · Paper page
  23. 10.1091/mbc.e11-11-0915 · DOI
  24. Longtine M, 1998, Yeast, 14, 953, 10.1002/(SICI)1097-0061(199807)14:10<953::AID-YEA293>3.0.CO;2-U · DOI
  25. Lucas M, 2016, Cell, 167, 1623, 10.1016/j.cell.2016.10.056 · DOI · Paper page
  26. Peter BJ, 2004, Science, 303, 495, 10.1126/science.1092586 · DOI · Paper page
  27. 10.1091/mbc.e16-08-0582 · DOI
  28. Pylypenko O, 2007, EMBO J, 26, 4788, 10.1038/sj.emboj.7601889 · DOI
  29. Rojas R, 2008, J Cell Biol, 183, 513, 10.1083/jcb.200804048 · DOI · Paper page
  30. Seaman M, 1997, J Cell Biol, 137, 79, 10.1083/jcb.137.1.79 · DOI · Paper page
  31. Seaman MNJ, 2012, J Cell Sci, 125, 4693, 10.1242/jcs.103440 · DOI · Paper page
  32. Seaman MNJ, 2013, Trends Cell Biol, 23, 522, 10.1016/j.tcb.2013.04.010 · DOI
  33. Seaman MNJ, 2009, J Cell Sci, 122, 2371, 10.1242/jcs.048686 · DOI · Paper page
  34. Simonetti B, 2017, J Cell Biol, 216, 3695, 10.1083/jcb.201703015 · DOI · Paper page
  35. Sorkin A, 2009, Nat Rev Mol Cell Biol, 10, 609, 10.1038/nrm2748 · DOI · Paper page
  36. Stachowiak JC, 2012, Nat Cell Biol, 14, 944, 10.1038/ncb2561 · DOI
  37. Steinberg F, 2013, Nat Cell Biol, 15, 1, 10.1038/ncb2667 · DOI
  38. Strochlic TI, 2007, J Cell Biol, 177, 115, 10.1083/jcb.200609161 · DOI · Paper page
  39. van Weering JRT, 2012, EMBO J, 31, 4466, 10.1038/emboj.2012.283 · DOI · Paper page
  40. van Weering JRT, 2012, Traffic, 13, 94, 10.1111/j.1600-0854.2011.01297.x · DOI
  41. Varandas KC, 2016, Curr Biol, 26, 3129, 10.1016/j.cub.2016.09.052 · DOI · Paper page

Cited by

Sorted by citations

Metadata

Authors
Purushothaman, L. K., & Ungermann, C.
Venue
Molecular Biology of the Cell
Published
2018-11
Volume
29
Issue
22
Pages
2709-2719
ISSN
  • 1059-1524
  • 1939-4586
Cited by
35
References
1
Language
en

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