Student or educator? Sign up with your school email and get 6 months of Pro free.
Cited by 748

The DOI matches its Crossref record; 7 of the 7 references it cites were found in a registry or an index.

The emerging shape of the ESCRT machinery

Williams, Roger L., Urbé, Sylvie·2007·Nature Reviews Molecular Cell Biology

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 · 10.1038/nrm2162

Cites

7 of 7 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

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

Show all 7 references

Research works printed but not linked: 131

  1. Luzio, J. P. et al. Lysosome-endosome fusion and lysosome biogenesis. J. Cell Sci. 113, 1515–1524 (2000). · DOI · Paper page
  2. Welsch, S. et al. Ultrastructural analysis of ESCRT proteins suggests a role for endosome-associated tubular–vesicular membranes in ESCRT function. Traffic 7, 1551–1566 (2006). · DOI
  3. Morita, E. & Sundquist, W. I. Retrovirus budding. Annu. Rev. Cell Dev. Biol. 20, 395–425 (2004). · DOI · Paper page
  4. Odorizzi, G. The multiple personalities of Alix. J. Cell Sci. 119, 3025–3032 (2006). · DOI
  5. Penalva, M. A. & Arst, H. N. Jr. Recent advances in the characterization of ambient pH regulation of gene expression in filamentous fungi and yeasts. Annu Rev. Microbiol. 58, 425–451 (2004). · DOI
  6. Clague, M. J. Membrane transport: a coat for ubiquitin. Curr. Biol. 12, R529–R531 (2002). · DOI
  7. Clague, M. & Urbe, S. Hrs function: viruses provide the clue. Trends Cell Biol. 13, 603–606 (2003). · DOI
  8. Bilodeau, P. S., Urbanowski, J. L., Winistorfer, S. C. & Piper, R. C. The Vps27p Hse1p complex binds ubiquitin and mediates endosomal protein sorting. Nature Cell Biol. 4, 534–539 (2002). · DOI · Paper page
  9. Raymond, C. K., Howald-Stevenson, I., Vater, C. A. & Stevens, T. H. Morphological classification of the yeast vacuolar protein sorting mutants: evidence for a prevacuolar compartment in class E vps mutants. Mol. Biol. Cell 3, 1389–1402 (1992). · DOI · Paper page
  10. Rieder, S. E., Banta, L. M., Kohrer, K., McCaffery, J. M. & Emr, S. D. Multilamellar endosome-like compartment accumulates in the yeast vps28 vacuolar protein sorting mutant. Mol. Biol. Cell 7, 985–999 (1996). · DOI · Paper page
  11. Lloyd, T. E. et al. Hrs regulates endosome membrane invagination and tyrosine kinase receptor signaling in Drosophila. Cell 108, 261–269 (2002). · DOI · Paper page
  12. Komada, M. & Soriano, P. Hrs, a FYVE finger protein localized to early endosomes, is implicated in vesicular traffic and required for ventral folding morphogenesis. Genes Dev. 13, 1475–1485 (1999). · DOI · Paper page
  13. Kanazawa, C. et al. Effects of deficiencies of STAMs and Hrs, mammalian class E Vps proteins, on receptor downregulation. Biochem. Biophys. Res. Commun. 309, 848–856 (2003). · DOI · Paper page
  14. Razi, M. & Futter, C. E. Distinct roles for Tsg101 and Hrs in multivesicular body formation and inward vesiculation. Mol. Biol. Cell 17, 3469–3483 (2006). · DOI · Paper page
  15. Hammond, D. E. et al. Endosomal dynamics of Met determine signaling output. Mol. Biol. Cell 14, 1346–1354 (2003). · DOI
  16. Bache, K., Raiborg, C., Mehlum, A. & Stenmark, H. STAM and Hrs are subunits of a multivalent ubiquitin-binding complex on early endosomes. J. Biol. Chem. 278, 12513–12521 (2003). · DOI · Paper page
  17. Gillooly, D. J. et al. Localization of phosphatidylinositol 3-phosphate in yeast and mammalian cells. EMBO J. 19, 4577–4588 (2000). · DOI · Paper page
  18. Raiborg, C. et al. FYVE and coiled-coil domains determine the specific localisation of Hrs to early endosomes. J. Cell Sci. 114, 2255–2263 (2001). · DOI · Paper page
  19. Urbe, S., Mills, I. G., Stenmark, H., Kitamura, N. & Clague, M. J. Endosomal localization and receptor dynamics determine tyrosine phosphorylation of hepatocyte growth factor-regulated tyrosine kinase substrate. Mol. Cell. Biol. 20, 7685–7692 (2000). · DOI
  20. Raiborg, C. et al. Hrs sorts ubiquitinated proteins into clathrin-coated microdomains of early endosomes. Nature Cell Biol. 4, 394–398 (2002). · DOI · Paper page
  21. Urbe, S. et al. The UIM domain of Hrs couples receptor sorting to vesicle formation. J. Cell Sci. 116, 4169–4179 (2003). · DOI · Paper page
  22. Murk, J. L. et al. Endosomal compartmentalization in three dimensions: implications for membrane fusion. Proc. Natl Acad. Sci. USA 100, 13332–13337 (2003). · DOI
  23. Sachse, M., Urbe, S., Oorschot, V., Strous, G. J. & Klumperman, J. Bilayered clathrin coats on endosomal vacuoles are involved in protein sorting toward lysosomes. Mol. Biol. Cell 13, 1313–1328 (2002). References 21 and 24 provide evidence that ubiquitylated receptors are sorted at endosomes via HRS and clathrin, and clathrin in turn restricts the distribution of HRS (reference 26). · DOI · Paper page
  24. McCullough, J. et al. Activation of the endosome-associated ubiquitin isopeptidase AMSH by STAM, a component of the multivesicular body-sorting machinery. Curr. Biol. 16, 160–165 (2006). · DOI
  25. Raiborg, C., Wesche, J., Malerod, L. & Stenmark, H. Flat clathrin coats on endosomes mediate degradative protein sorting by scaffolding Hrs in dynamic microdomains. J. Cell Sci. 119, 2414–2424 (2006). · DOI
  26. Asao, H. et al. Hrs is associated with STAM, a signal-transducing adaptor molecule. Its suppressive effect on cytokine-induced cell growth. J. Biol. Chem. 272, 32785–32791 (1997). · DOI · Paper page
  27. Takata, H., Kato, M., Denda, K. & Kitamura, N. A Hrs binding protein having a Src homology 3 domain is involved in intracellular degradation of growth factors and their receptors. Genes Cells 5, 57–69 (2000). · DOI · Paper page
  28. Kobayashi, H. et al. Hrs, a mammalian master molecule in vesicular transport and protein sorting, suppresses the degradation of ESCRT proteins signal transducing adaptor molecule 1 and 2. J. Biol. Chem. 280, 10468–10477 (2005). · DOI
  29. Mizuno, E., Kawahata, K., Okamoto, A., Kitamura, N. & Komada, M. Association with Hrs is required for the early endosomal localization, stability, and function of STAM. J. Biochem. 135, 385–396 (2004). · DOI
  30. Mao, Y. et al. Crystal structure of the VHS and FYVE tandem domains of Hrs, a protein involved in membrane trafficking and signal transduction. Cell 100, 447–456 (2000). · DOI · Paper page
  31. Hanyaloglu, A., McCullagh, E. & von Zastrow, M. Essential role of Hrs in a recycling mechanism mediating functional resensitization of cell signaling. EMBO J. 24, 2265–2283 (2005). · DOI · Paper page
  32. Mizuno, E., Kawahata, K., Kato, M., Kitamura, N. & Komada, M. STAM proteins bind ubiquitinated proteins on the early endosome via the VHS domain and ubiquitin-interacting motif. Mol. Biol. Cell 14, 3675–3689 (2003). · DOI
  33. Misra, S. & Hurley, J. H. Crystal structure of a phosphatidylinositol 3-phosphate-specific membrane-targeting motif, the FYVE domain of Vps27p. Cell 97, 657–666 (1999). · DOI · Paper page
  34. Dumas, J. J. et al. Multivalent endosome targeting by homodimeric EEA1. Mol. Cell 8, 947–958 (2001). · DOI · Paper page
  35. Stahelin, R. V. et al. Phosphatidylinositol-3-phosphate induces the membrane penetration of the FYVE domains of Vps27p and Hrs. J. Biol. Chem. 277, 26379–26388 (2002). · DOI · Paper page
  36. Pullan, L. et al. The endosome-associated protein Hrs is hexameric and controls cargo sorting as a “master molecule”. Structure 14, 661–671 (2006). · DOI
  37. Lu, Q., Hope, L. W., Brasch, M., Reinhard, C. & Cohen, S. N. TSG101 interaction with HRS mediates endosomal trafficking and receptor down-regulation. Proc. Natl Acad. Sci. USA 100, 7626–7631 (2003). · DOI · Paper page
  38. Bache, K. G., Brech, A., Mehlum, A. & Stenmark, H. Hrs regulates multivesicular body formation via ESCRT recruitment to endosomes. J. Cell Biol. 162, 435–442 (2003). · DOI · Paper page
  39. Pornillos, O., Alam, S., Davis, D. & Sundquist, W. Structure of the Tsg101 UEV domain in complex with the PTAP motif of the HIV-1 p6 protein. Nature Struct. Biol. 9, 812–817 (2002).
  40. Pornillos, O. et al. Structure and functional interactions of the Tsg101 UEV domain. EMBO J. 21, 2397–2406 (2002). · DOI · Paper page
  41. Pornillos, O. et al. HIV Gag mimics the Tsg101-recruiting activity of the human Hrs protein. J. Cell Biol. 162, 425–434 (2003). · DOI · Paper page
  42. Katzmann, D., Stefan, C., Babst, M. & Emr, S. Vps27 recruits ESCRT machinery to endosomes during MVB sorting. J. Cell Biol. 162, 413–423 (2003). · DOI · Paper page
  43. Bilodeau, P., Winistorfer, S., Kearney, W., Robertson, A. & Piper, R. Vps27–Hse1 and ESCRT-I complexes cooperate to increase efficiency of sorting ubiquitinated proteins at the endosome. J. Cell Biol. 163, 237–243 (2003). · DOI · Paper page
  44. Katzmann, D., Babst, M. & Emr, S. Ubiquitin-dependent sorting into the multivesicular body pathway requires the function of a conserved endosomal protein sorting complex, ESCRT-I. Cell 106, 145–155 (2001). · DOI · Paper page
  45. Oestreich, A. J., Davies, B. A., Payne, J. A. & Katzmann, D. J. Mvb12 is a novel member of ESCRT-I involved in cargo selection by the MVB pathway. Mol. Biol. Cell 18, 646–657 (2006). · DOI
  46. Chu, T., Sun, J., Saksena, S. & Emr, S. D. New component of ESCRT-I regulates endosomal sorting complex assembly. J. Cell Biol. 175, 815–823 (2006). · DOI
  47. Curtiss, M., Jones, C. & Babst, M. Efficient cargo sorting by ESCRT-I and the subsequent release of ESCRT-I from MVBs requires the subunit Mvb12. Mol. Biol. Cell 18, 636–645 (2007). · DOI
  48. Gill, D. J. et al. Structural insight into the ESCRT-I/-II link and its role in MVB trafficking. EMBO J. 26, 600–612 (2007). · DOI
  49. Bache, K. G. et al. The growth-regulatory protein HCRP1/hVps37A is a subunit of mammalian ESCRT-I and mediates receptor downregulation. Mol. Biol. Cell 15, 4337–4346 (2004). · DOI · Paper page
  50. Eastman, S. W., Martin-Serrano, J., Chung, W., Zang, T. & Bieniasz, P. D. Identification of human VPS37C, a component of endosomal sorting complex required for transport-I important for viral budding. J. Biol. Chem. 280, 628–636 (2005). · DOI
  51. Stuchell, M. D. et al. The human endosomal sorting complex required for transport (ESCRT-I) and its role in HIV-1 budding. J. Biol. Chem. 279, 36059–36071 (2004). · DOI
  52. Doyotte, A., Russell, M. R., Hopkins, C. R. & Woodman, P. G. Depletion of TSG101 forms a mammalian “Class E” compartment: a multicisternal early endosome with multiple sorting defects. J. Cell Sci. 118, 3003–3017 (2005). References 15 and 54 show that in mammalian cells ESCRT-I depletion results in extensive tubulation and prevents ILVs formation, whereas HRS depletion produces enlarged, spherical MVBs with few ILVs. · DOI · Paper page
  53. Feng, G. H., Lih, C. J. & Cohen, S. N. TSG101 protein steady-state level is regulated posttranslationally by an evolutionarily conserved COOH-terminal sequence. Cancer Res. 60, 1736–1741 (2000).
  54. Teo, H., Veprintsev, D. B. & Williams, R. L. Structural insights into endosomal sorting complex required for transport (ESCRT-I) recognition of ubiquitinated proteins. J. Biol. Chem. 279, 28689–28696 (2004). · DOI
  55. Sundquist, W. I. et al. Ubiquitin recognition by the human TSG101 protein. Mol. Cell 13, 783–789 (2004). · DOI · Paper page
  56. Pineda-Molina, E. et al. The crystal structure of the C-terminal domain of Vps28 reveals a conserved surface required for Vps20 recruitment. Traffic 7, 1007–1016 (2006). · DOI
  57. Langelier, C. et al. Human ESCRT-II complex and its role in human immunodeficiency virus type 1 release. J. Virol. 80, 9465–9680 (2006). · DOI · Paper page
  58. Babst, M., Katzmann, D. J., Snyder, W. B., Wendland, B. & Emr, S. D. Endosome-associated complex, ESCRT-II, recruits transport machinery for protein sorting at the multivesicular body. Dev. Cell 3, 283–289 (2002). · DOI · Paper page
  59. Teo, H., Perisic, O., Gonzalez, B. & Williams, R. L. ESCRT-II, an endosome-associated complex required for protein sorting: crystal structure and interactions with ESCRT-III and membranes. Dev. Cell 7, 559–569 (2004). · DOI
  60. Hierro, A. et al. Structure of the ESCRT-II endosomal trafficking complex. Nature 431, 221–225 (2004). References 55, 56, 63 and 64 show the structural organization of multisubunit ESCRT-I and -II cores, as well as the structure of the ESCRT-II Ptdins3P-binding GLUE domain, and demonstrate a direct link between yeast ESCRT-I and ESCRT-II. · DOI · Paper page
  61. Wernimont, A. K. & Weissenhorn, W. Crystal structure of subunit VPS25 of the endosomal trafficking complex ESCRT-II. BMC Struct. Biol. 4, 10 (2004). · DOI
  62. Yorikawa, C. et al. Human CHMP6, a myristoylated ESCRT-III protein, interacts directly with an ESCRT-II component EAP20 and regulates endosomal cargo sorting. Biochem. J. 387, 17–26 (2005). · DOI
  63. Slagsvold, T. et al. Eap45 in mammalian ESCRT-II binds ubiquitin via a phosphoinositide-interacting GLUE domain. J. Biol. Chem. 280, 19600–19606 (2005). · DOI · Paper page
  64. Hirano, S. et al. Structural basis of ubiquitin recognition by mammalian Eap45 GLUE domain. Nature Struct. Mol. Biol. 13, 1031–1032 (2006). · DOI
  65. Alam, S. L. et al. Structural basis for ubiquitin recognition by the human ESCRT-II EAP45 GLUE domain. Nature Struct. Mol. Biol. 13, 1029–1030 (2006). · DOI
  66. Alam, S. L. et al. Ubiquitin interactions of NZF zinc fingers. EMBO J. 23, 1411–1421 (2004). · DOI · Paper page
  67. Thompson, B. J. et al. Tumor suppressor properties of the ESCRT-II complex component Vps25 in Drosophila. Dev. Cell 9, 711–720 (2005). · DOI · Paper page
  68. Herz, H. M. et al. vps25 mosaics display non-autonomous cell survival and overgrowth, and autonomous apoptosis. Development 133, 1871–1880 (2006). · DOI
  69. Vaccari, T. & Bilder, D. The Drosophila tumor suppressor Vps25 prevents nonautonomous overproliferation by regulating notch trafficking. Dev. Cell 9, 687–698 (2005). References 71, 72 and 73 demonstrate an important role for ESCRT-II in metazoan cells. · DOI · Paper page
  70. Moberg, K. H., Schelble, S., Burdick, S. K. & Hariharan, I. K. Mutations in erupted, the Drosophila ortholog of mammalian tumor susceptibility gene 101, elicit non-cell-autonomous overgrowth. Dev. Cell 9, 699–710 (2005). · DOI · Paper page
  71. Bowers, K. et al. Degradation of endocytosed epidermal growth factor and virally ubiquitinated major histocompatibility complex class I is independent of mammalian ESCRTII. J. Biol. Chem. 281, 5094–5105 (2006). · DOI · Paper page
  72. Babst, M., Katzmann, D. J., Estepa-Sabal, E. J., Meerloo, T. & Emr, S. D. ESCRT-III: an endosome-associated heterooligomeric protein complex required for MVB sorting. Dev. Cell 3, 271–282 (2002). References 45, 62 and 76 first defined the functions and compositions of ESCRT-I, -II and -III, respectively. · DOI · Paper page
  73. Amerik, A., Nowak, J., Swaminathan, S. & Hochstrasser, M. The Doa4 deubiquitinating enzyme is functionally linked to the vacuolar protein-sorting and endocytic pathways. Mol. Biol. Cell 11, 3365–3380 (2000). References 77, 111 and 113 demonstrate a requirement for a DUB in the endocytic pathway in yeast. · DOI · Paper page
  74. Kranz, A., Kinner, A. & Kolling, R. A family of small coiled-coil-forming proteins functioning at the late endosome in yeast. Mol. Biol. Cell 12, 711–723 (2001). · DOI
  75. Howard, T. L., Stauffer, D. R., Degnin, C. R. & Hollenberg, S. M. CHMP1 functions as a member of a newly defined family of vesicle trafficking proteins. J. Cell Sci. 114, 2395–2404 (2001). · DOI
  76. Nickerson, D. P., West, M. & Odorizzi, G. Did2 coordinates Vps4-mediated dissociation of ESCRT-III from endosomes. J. Cell Biol. 175, 715–720 (2006). Reference 80 demonstrates that Did2 has an important role in Vps4-mediated disassembly of ESCRT-III but not of ESCRT-I and-II, that ILV formation can be uncoupled from ESCRT-III disassembly and that class E compartments can have either multilammelar structures without ILVs ( vps4Δ ) or tubular structures with ILVs ( did2Δ). · DOI · Paper page
  77. Horii, M. et al. CHMP7, a novel ESCRT-III-related protein, associates with CHMP4b and functions in the endosomal sorting pathway. Biochem. J. 400, 23–32 (2006). · DOI
  78. Muziol, T. et al. Structural basis for budding by the ESCRT-III factor CHMP3. Dev. Cell 10, 821–830 (2006). The structure of an ESCRT-III subunit provides a model for how activated subunits might assemble into dimers and arrays. · DOI
  79. Zamborlini, A. et al. Release of autoinhibition converts ESCRT-III components into potent inhibitors of HIV-1 budding. Proc. Natl Acad. Sci. USA 103, 19140–19145 (2006). · DOI
  80. Agromayor, M. & Martin-Serrano, J. Interaction of AMSH with ESCRT-III and deubiquitination of endosomal cargo. J. Biol. Chem. 281, 23083–23091 (2006). · DOI
  81. McCullough, J., Clague, M. J. & Urbe, S. AMSH is an endosome-associated ubiquitin isopeptidase. J. Cell Biol. 166, 487–492 (2004). Reference 85 shows that AMSH is a Lys63-ubiquitin-chain specific DUB that has a role in sorting a growth-factor receptor at endosomes, and is recruited to CHMPs (shown in references 25, 84 and 88). · DOI · Paper page
  82. Scott, A. et al. Structural and mechanistic studies of VPS4 proteins. EMBO J. 24, 3658–3669 (2005). Structure-based mutagenesis suggests that during their disassembly by VPS4, ESCRT-III subunits are pulled into a central pore of the VPS4 double ring after the initial capture of ESCRT-III subunits by a three-helix bundle of VPS4 MIT domain (shown in reference 95). · DOI · Paper page
  83. von Schwedler, U. K. et al. The protein network of HIV budding. Cell 114, 701–713 (2003). References 87 and 90 were the first to characterize the network of interactions among the human ESCRT components and to show their roles in HIV-1 budding. · DOI · Paper page
  84. Tsang, H. T. et al. A systematic analysis of human CHMP protein interactions: additional MIT domain-containing proteins bind to multiple components of the human ESCRT III complex. Genomics 88, 333–346 (2006). · DOI
  85. Bowers, K. et al. Protein–protein interactions of ESCRT complexes in the yeast Saccharomyces cerevisiae. Traffic 5, 194–210 (2004). · DOI
  86. Martin-Serrano, J., Yarovoy, A., Perez-Caballero, D. & Bieniasz, P. D. Divergent retroviral late-budding domains recruit vacuolar protein sorting factors by using alternative adaptor proteins. Proc. Natl Acad. Sci. USA 100, 12414–12419 (2003). · DOI · Paper page
  87. Lin, Y., Kimpler, L. A., Naismith, T. V., Lauer, J. M. & Hanson, P. I. Interaction of the mammalian endosomal sorting complex required for transport (ESCRT) III protein hSnf7–1 with itself, membranes, and the AAA+ ATPase SKD1. J. Biol. Chem. 280, 12799–12809 (2005). · DOI
  88. Eugster, A. et al. Ent5p is required with Ent3p and Vps27p for ubiquitin-dependent protein sorting into the multivesicular body. Mol. Biol. Cell 15, 3031–3041 (2004). · DOI
  89. Whitley, P. et al. Identification of mammalian Vps24p as an effector of phosphatidylinositol-3,5-bisphosphate-dependent endosome compartmentalization. J. Biol. Chem. 278, 38786–38795 (2003). · DOI
  90. Kyuuma, M. et al. AMSH, an ESCRT-III associated enzyme, deubiquitinates cargo on MVB/late endosomes. Cell Struct. Funct. 31, 159–172 (2007). · DOI
  91. Scott, A. et al. Structure and ESCRT-III protein interactions of the MIT domain of human VPS4A. Proc. Natl Acad. Sci. USA 102, 13813–13818 (2005). · DOI · Paper page
  92. Ward, D. M. et al. The role of LIP5 and CHMP5 in multivesicular body formation and HIV-1 budding in mammalian cells. J. Biol. Chem. 280, 10548–10555 (2005). · DOI
  93. Bache, K. G. et al. The ESCRT-III subunit hVps24 is required for degradation but not silencing of the epidermal growth factor receptor. Mol. Biol. Cell 17, 2513–2523 (2006). · DOI
  94. Shim, J. H. et al. CHMP5 is essential for late endosome function and down-regulation of receptor signaling during mouse embryogenesis. J. Cell Biol. 172, 1045–1056 (2006). · DOI
  95. Azmi, I. et al. Recycling of ESCRTs by the AAA-ATPase Vps4 is regulated by a conserved VSL region in Vta1. J. Cell Biol. 172, 705–717 (2006). · DOI
  96. Sachse, M., Strous, G. J. & Klumperman, J. ATPase-deficient hVPS4 impairs formation of internal endosomal vesicles and stabilizes bilayered clathrin coats on endosomal vacuoles. J. Cell Sci. 117, 1699–1708 (2004). · DOI
  97. Scheuring, S. et al. Mammalian cells express two VPS4 proteins both of which are involved in intracellular protein trafficking. J. Mol. Biol. 312, 469–480 (2001). · DOI
  98. Babst, M., Wendland, B., Estepa, E. J. & Emr, S. D. The Vps4p AAA ATPase regulates membrane association of a Vps protein complex required for normal endosome function. EMBO J. 17, 2982–2993 (1998). · DOI · Paper page
  99. Fujita, H. et al. A dominant negative form of the AAA ATPase SKD1/VPS4 impairs membrane trafficking out of endosomal/lysosomal compartments: class E vps phenotype in mammalian cells. J. Cell Sci. 116, 401–414 (2003). · DOI
  100. DeLaBarre, B., Christianson, J. C., Kopito, R. R. & Brunger, A. T. Central pore residues mediate the p97/VCP activity required for ERAD. Mol. Cell 22, 451–462 (2006). · DOI
  101. Fujita, H. et al. Mammalian class E Vps proteins, SBP1 and mVps2/CHMP2A, interact with and regulate the function of an AAA-ATPase SKD1/Vps4B. J. Cell Sci. 117, 2997–3009 (2004). · DOI
  102. Yeo, S. C. et al. Vps20p and Vta1p interact with Vps4p and function in multivesicular body sorting and endosomal transport in Saccharomyces cerevisiae. J. Cell Sci. 116, 3957–3970 (2003). · DOI
  103. Shiflett, S. et al. Characterization of Vta1p, a class E Vps protein in Saccharomyces cerevisiae. J. Biol. Chem. 279, 10982–10990 (2004). · DOI
  104. Luhtala, N. & Odorizzi, G. Bro1 coordinates deubiquitination in the multivesicular body pathway by recruiting Doa4 to endosomes. J. Cell Biol. 166, 717–729 (2004). · DOI · Paper page
  105. Amerik, A. Y. & Hochstrasser, M. Mechanism and function of deubiquitinating enzymes. Biochim. Biophys. Acta 1695, 189–207 (2004). · DOI · Paper page
  106. Losko, S., Kopp, F., Kranz, A. & Kolling, R. Uptake of the ATP-binding cassette (ABC) transporter Ste6 into the yeast vacuole is blocked in the doa4 mutant. Mol. Biol. Cell 12, 1047–1059 (2001). · DOI
  107. Reggiori, F. & Pelham, H. R. B. Sorting of proteins into multivesicular bodies: ubiquitin-dependent and-independent targeting. EMBO J. 20, 5176–5186 (2001). Shows that although ubiquitin functions as a key signal for the sorting of membrane proteins into the MVBs, ubiquitin-independent sorting can also occur. · DOI · Paper page
  108. Dupre, S. & Haguenauer-Tsapis, R. Deubiquitination step in the endocytic pathway of yeast plasma membrane proteins: crucial role of Doa4p ubiquitin isopeptidase. Mol. Cell. Biol. 21, 4482–4494 (2001). · DOI
  109. Avvakumov, G. V. et al. Amino-terminal dimerization, NRDP1-rhodanese interaction, and inhibited catalytic domain conformation of the ubiquitin-specific protease 8 (USP8). J. Biol. Chem. 281, 38061–38070 (2006). · DOI · Paper page
  110. Hu, M. et al. Crystal structure of a UBP-family deubiquitinating enzyme in isolation and in complex with ubiquitin aldehyde. Cell 111, 1041–1054 (2002). · DOI · Paper page
  111. Kato, M., Miyazawa, K. & Kitamura, N. A deubiquitinating enzyme UBPY interacts with the Src homology 3 domain of Hrs-binding protein via a novel binding motif PX(V/I)(D/N)RXXKP. J. Biol. Chem. 275, 37481–37487 (2000). · DOI · Paper page
  112. Kaneko, T. et al. Structural insight into modest binding of a non-PXXP ligand to the signal transducing adaptor molecule-2 Src homology 3 domain. J. Biol. Chem. 278, 48162–48168 (2003). · DOI · Paper page
  113. Ren, J., Kee, Y., Huibregtse, J. M. & Piper, R. C. Hse1, a component of the yeast Hrs-STAM ubiquitin sorting complex, associates with ubiquitin peptidases and a ligase to control sorting efficiency into multivesicular bodies. Mol. Biol. Cell 18, 324–335 (2007). · DOI · Paper page
  114. Row, P. E., Prior, I. A., McCullough, J., Clague, M. J. & Urbe, S. The ubiquitin isopeptidase UBPY regulates endosomal ubiquitin dynamics and is essential for receptor down-regulation. J. Biol. Chem. 281, 12618–12624 (2006). · DOI · Paper page
  115. Mizuno, E., Kobayashi, K., Yamamoto, A., Kitamura, N. & Komada, M. A deubiquitinating enzyme UBPY regulates the level of protein ubiquitination on endosomes. Traffic 7, 1017–1031 (2006). References 120, 121 and 75 report on a key role for the DUB UBPY in receptor downregulation and endosomal ubiquitin dynamics. · DOI
  116. Alwan, H. A. & van Leeuwen, J. E. UBPY-mediated epidermal growth factor receptor (EGFR) de-ubiquitination promotes EGFR degradation. J. Biol. Chem. 282, 1658–1669 (2007). · DOI · Paper page
  117. Kee, Y., Munoz, W., Lyon, N. & Huibregtse, J. M. The Ubp2 deubiquitinating enzyme modulates Rsp5-dependent K63-linked polyubiquitin conjugates in Saccharomyces cerevisiae. J. Biol. Chem. 281, 36724–36731 (2006). · DOI
  118. Rink, J., Ghigo, E., Kalaidzidis, Y. & Zerial, M. Rab conversion as a mechanism of progression from early to late endosomes. Cell 122, 735–749 (2005). · DOI · Paper page
  119. Rusten, T. E. et al. Fab1 phosphatidylinositol 3-phosphate 5-kinase controls trafficking but not silencing of endocytosed receptors. Mol. Biol. Cell 17, 3989–4001 (2006). · DOI
  120. White, I. J., Bailey, L. M., Aghakhani, M. R., Moss, S. E. & Futter, C. E. EGF stimulates annexin 1-dependent inward vesiculation in a multivesicular endosome subpopulation. EMBO J. 25, 1–12 (2006). · DOI · Paper page
  121. Field, M. C., Gabernet-Castello, C. & Dacks, J. B. in Origins and Evolution of Eukaryotic Endomembranes and Cytoskeleton (ed. Jékely, G.) (Landes Bioscience, Austin 2007).
  122. Slater, R. & Bishop, N. E. Genetic structure and evolution of the Vps25 family, a yeast ESCRT-II component. BMC Evol. Biol. 6, 59 (2006). · DOI
  123. Yang, M. et al. The Plasmodium falciparum Vps4 homolog mediates multivesicular body formation. J. Cell Sci. 117, 3831–3838 (2004). · DOI
  124. Fisher, R. D. et al. Structure and ubiquitin binding of the ubiquitin-interacting motif. J. Biol. Chem. 278, 28976–28984 (2003). · DOI · Paper page
  125. Madshus, I. H. Ubiquitin binding in endocytosis — how tight should it be and where does it happen? Traffic 7, 258–261 (2006). · DOI
  126. Hirano, S. et al. Double-sided ubiquitin binding of Hrs-UIM in endosomal protein sorting. Nature Struct. Mol. Biol. 13, 272–277 (2006). · DOI · Paper page
  127. Swanson, K. A., Kang, R. S., Stamenova, S. D., Hicke, L. & Radhakrishnan, I. Solution structure of Vps27 UIM–ubiquitin complex important for endosomal sorting and receptor downregulation. EMBO J. 22, 4597–4606 (2003). · DOI · Paper page
  128. Misra, S., Miller, G. J. & Hurley, J. H. Recognizing phosphatidylinositol 3-phosphate. Cell 107, 559–562 (2001). · DOI
  129. Johnson, E. E., Overmeyer, J. H., Gunning, W. T. & Maltese, W. A. Gene silencing reveals a specific function of hVps34 phosphatidylinositol 3-kinase in late versus early endosomes. J. Cell Sci. 119, 1219–1232 (2006). · DOI
  130. Futter, C. E., Collinson, L. M., Backer, J. M. & Hopkins, C. R. Human VPS34 is required for internal vesicle formation within multivesicular endosomes. J. Cell Biol. 155, 1251–1264 (2001). · DOI · Paper page
  131. Bruckmann, A., Kunkel, W., Augsten, K., Wetzker, R. & Eck, R. The deletion of CaVPS34 in the human pathogenic yeast Candida albicans causes defects in vesicle-mediated protein sorting and nuclear segregation. Yeast 18, 343–353 (2001). · doi:10.1002/1097-0061(20010315)18:4<343::aid-yea675>3.0.co;2-z

Cited by

See all 748

Metadata

Authors
Williams, R. L., & Urbé, S.
Venue
Nature Reviews Molecular Cell Biology
Published
2007-05
Volume
8
Issue
5
Pages
355-368
ISSN
  • 1471-0072 (ISSN-L)
  • 1471-0080
OpenAlex
W1990741894
Cited by
748
References
7
FWCI
3.90
Type
journal article
Language
en
Open access
closed
Licence
www.springer.com/tdm (tdm)

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

How to cite

Cite CoChat for the checks on this page, and the paper for its own findings.

This page
CoChat. (2026). Citation check: The emerging shape of the ESCRT machinery. https://app.cochat.ai/papers/10.1038/nrm2162
The paper
Williams, R. L., & Urbé, S. (2007). The emerging shape of the ESCRT machinery. Nature Reviews Molecular Cell Biology. https://doi.org/10.1038/nrm2162

Data sources

Bibliographic data: Semantic Scholar, OpenAlex, Crossref.

Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.