Cited by 143

The DOI matches its Crossref record; 4 of the 4 references it cites were found in a registry or an index.

Epsins: adaptors in endocytosis?

Wendland, Beverly·2002·Nature Reviews Molecular Cell Biology

Abstract

Endocytic adaptor proteins select specific cargo for internalization by endocytosis through clathrin-coated pits or vesicles. Recent studies indicate that epsins might also be classified as adaptors.

Overview

Integrity signals

Registry

Crossref · 10.1038/nrm970

Cites

4 of 4 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?

Citations

Cites

Flagged first, then by citations

Show all 4 references

Research works printed but not linked: 71

  1. Brodsky, F. M., Chen, C. Y., Knuehl, C., Towler, M. C. & Wakeham, D. E. Biological basket weaving: formation and function of clathrin-coated vesicles. Annu. Rev. Cell Dev. Biol. 17, 517–568 (2001). · DOI
  2. Pearse, B. M. Receptors compete for adaptors found in plasma membrane coated pits. EMBO J. 7, 3331–3336 (1988). · DOI
  3. Kirchhausen, T. Adaptors for clathrin-mediated traffic. Annu. Rev. Cell Dev. Biol. 15, 705–732 (1999). · DOI · Paper page
  4. Gaidarov, I., Krupnick, J. G., Falck, J. R., Benovic, J. L. & Keen, J. H. Arrestin function in G protein-coupled receptor endocytosis requires phosphoinositide binding. EMBO J. 18, 871–881 (1999). · DOI
  5. Goodman, O. B. Jr. et al. β-arrestin acts as a clathrin adaptor in endocytosis of the β2-adrenergic receptor. Nature 383, 447–450 (1996). · DOI
  6. Chen, H. et al. Epsin is an EH-domain-binding protein implicated in clathrin-mediated endocytosis. Nature 394, 793–797 (1998). · DOI · Paper page
  7. Wendland, B., Steece, K. E. & Emr, S. D. Yeast epsins contain an essential N-terminal ENTH domain, bind clathrin and are required for endocytosis. EMBO J. 18, 4383–4393 (1999). · DOI
  8. De Camilli, P. et al. The ENTH domain. FEBS Lett. 513, 11–18 (2002). · DOI
  9. Shih, S. C. et al. Epsins and Vps27p/Hrs contain ubiquitin-binding domains that function in receptor endocytosis. Nature Cell Biol. 4, 389–393 (2002). · DOI
  10. Kay, B. K., Yamabhai, M., Wendland, B. & Emr, S. D. Identification of a novel domain shared by putative components of the endocytic and cytoskeletal machinery. Protein Sci. 8, 435–438 (1999). · DOI
  11. Itoh, T. et al. Role of the ENTH domain in phosphatidylinositol-4,5-bisphosphate binding and endocytosis. Science 291, 1047–1051 (2001). · DOI · Paper page
  12. Hyman, J., Chen, H., Di Fiore, P. P., De Camilli, P. & Brunger, A. T. Epsin 1 undergoes nucleocytosolic shuttling and its eps15 interactor NH2-terminal homology (ENTH) domain, structurally similar to Armadillo and HEAT repeats, interacts with the transcription factor promyelocytic leukemia Zn2+ finger protein (PLZF). J. Cell Biol. 149, 537–546 (2000). · DOI · Paper page
  13. Lohi, O. & Lehto, V. P. VHS domain marks a group of proteins involved in endocytosis and vesicular trafficking. FEBS Lett. 440, 255–257 (1998). · DOI
  14. Puertollano, R., Aguilar, R. C., Gorshkova, I., Crouch, R. J. & Bonifacino, J. S. Sorting of mannose 6-phosphate receptors mediated by the GGAs. Science 292, 1712–1716 (2001). · DOI · Paper page
  15. Takatsu, H., Katoh, Y., Shiba, Y. & Nakayama, K. Golgi-localizing, γ-adaptin ear homology domain, ADP-ribosylation factor-binding (GGA) proteins interact with acidic dileucine sequences within the cytoplasmic domains of sorting receptors through their Vps27p/Hrs/STAM (VHS) domains. J. Biol. Chem. 276, 28541–28545 (2001). · DOI
  16. Hofmann, K. & Falquet, L. A ubiquitin-interacting motif conserved in components of the proteasomal and lysosomal protein degradation systems. Trends Biochem. Sci. 26, 347–350 (2001). · DOI
  17. Oldham, C. E., Mohney, R. P., Miller, S. L., Hanes, R. N. & O'Bryan, J. P. The ubiquitin-interacting motifs target the endocytic adaptor protein epsin for ubiquitination. Curr. Biol. 12, 1112–1116 (2002). · DOI
  18. Klapisz, E. et al. A ubiquitin–interacting motif (UIM) is essential for Eps15 and Eps15R ubiquitination. J. Biol. Chem. 34, 30746–30753 (2002). · DOI
  19. Polo, S. et al. A single motif responsible for ubiquitin recognition and monoubiquitination in endocytic proteins. Nature 416, 451–455 (2002). · DOI · Paper page
  20. Hofmann, K. & Bucher, P. The UBA domain: a sequence motif present in multiple enzyme classes of the ubiquitination pathway. Trends Biochem. Sci. 21, 172–173 (1996). · DOI
  21. Buchberger, A. From UBA to UBX: new words in the ubiquitin vocabulary. Trends Cell Biol. 12, 216–221 (2002). · DOI
  22. Dell'Angelica, E. C. Clathrin-binding proteins: got a motif? Join the network! Trends Cell Biol. 11, 315–318 (2001). · DOI · Paper page
  23. Lafer, E. M. Clathrin-protein interactions. Traffic 3, 513–520 (2002). · DOI
  24. Salcini, A. E. et al. Binding specificity and in vivo targets of the EH domain, a novel protein–protein interaction module. Genes Dev. 11, 2239–2249 (1997). · DOI · Paper page
  25. Brett, T. J., Traub, L. M. & Fremont, D. H. Accessory protein recruitment motifs in clathrin-mediated endocytosis. Structure (Camb.) 10, 797–809 (2002). · DOI
  26. Kalthoff, C., Alves, J., Urbanke, C., Knorr, R. & Ungewickell, E. J. Unusual structural organization of the endocytic proteins AP180 and epsin 1. J. Biol. Chem. 277, 8209–8216 (2002). · DOI
  27. ter Haar, E., Musacchio, A., Harrison, S. C. & Kirchhausen, T. Atomic structure of clathrin: a β propeller terminal domain joins an α zigzag linker. Cell 95, 563–573 (1998). · DOI
  28. Pearse, B. M. & Robinson, M. S. Purification and properties of 100-kd proteins from coated vesicles and their reconstitution with clathrin. EMBO J. 3, 1951–1957 (1984). · DOI · Paper page
  29. Ahle, S. & Ungewickell, E. Purification and properties of a new clathrin assembly protein. EMBO J. 5, 3143–3149 (1986). · DOI
  30. Beck, K. A. & Keen, J. H. Interaction of phosphoinositide cycle intermediates with the plasma membrane-associated clathrin assembly protein AP-2. J. Biol. Chem. 266, 4442–4447 (1991). · DOI
  31. Norris, F. A., Ungewickell, E. & Majerus, P. W. Inositol hexakisphosphate binds to clathrin assembly protein 3 (AP- 3/AP180) and inhibits clathrin cage assembly in vitro. J. Biol. Chem. 270, 214–217 (1995). · DOI
  32. Ye, W., Ali, N., Bembenek, M. E., Shears, S. B. & Lafer, E. M. Inhibition of clathrin assembly by high affinity binding of specific inositol polyphosphates to the synapse-specific clathrin assembly protein AP-3. J. Biol. Chem. 270, 1564–1568 (1995). · DOI
  33. Yamabhai, M. et al. Intersectin, a novel adaptor protein with two Eps15 homology and five Src homology 3 domains. J. Biol. Chem. 273, 31401–31407 (1998). · DOI · Paper page
  34. Kariya, K. et al. Regulation of complex formation of POB1/epsin/adaptor protein complex 2 by mitotic phosphorylation. J. Biol. Chem. 275, 18399–18406 (2000). · DOI
  35. Watson, H. A., Cope, M. J., Groen, A. C., Drubin, D. G. & Wendland, B. In vivo role for actin-regulating kinases in endocytosis and yeast epsin phosphorylation. Mol. Biol. Cell 12, 3668–3679 (2001). · DOI
  36. Traub, L. M., Downs, M. A., Westrich, J. L. & Fremont, D. H. Crystal structure of the α appendage of AP-2 reveals a recruitment platform for clathrin-coat assembly. Proc. Natl Acad. Sci. USA 96, 8907–8912 (1999). · DOI
  37. Owen, D. J. et al. A structural explanation for the binding of multiple ligands by the α-adaptin appendage domain. Cell 97, 805–815 (1999). · DOI
  38. Zeng, G. & Cai, M. Regulation of the actin cytoskeleton organization in yeast by a novel serine/threonine kinase Prk1p. J Cell Biol 144, 71–82 (1999). · DOI
  39. Yeung, B. G., Phan, H. L. & Payne, G. S. Adaptor complex-independent clathrin function in yeast. Mol. Biol. Cell 10, 3643–3659 (1999). · DOI
  40. Wendland, B. & Emr, S. D. Pan1p, yeast eps15, functions as a multivalent adaptor that coordinates protein–protein interactions essential for endocytosis. J. Cell Biol. 141, 71–84 (1998). · DOI
  41. Baggett, J. J. & Wendland, B. Clathrin function in yeast endocytosis. Traffic 2, 297–302 (2001). · DOI
  42. Huang, K. M., D'Hondt, K., Riezman, H. & Lemmon, S. K. Clathrin functions in the absence of heterotetrameric adaptors and AP180-related proteins in yeast. EMBO J. 18, 3897–3908. (1999). · DOI
  43. Mullins, C. & Bonifacino, J. S. Structural requirements for function of yeast GGAs in vacuolar protein sorting, α-factor maturation, and interactions with clathrin. Mol. Cell. Biol. 21, 7981–7994 (2001). · DOI
  44. Costaguta, G., Stefan, C. J., Bensen, E. S., Emr, S. D. & Payne, G. S. Yeast Gga coat proteins function with clathrin in Golgi to endosome transport. Mol. Biol. Cell 12, 1885–1896 (2001). · DOI
  45. Cadavid, A. L., Ginzel, A. & Fischer, J. A. The function of the Drosophila fat facets deubiquitinating enzyme in limiting photoreceptor cell number is intimately associated with endocytosis. Development 127, 1727–1736 (2000). · DOI
  46. Chen, X., Zhang, B. & Fischer, J. A. A specific protein substrate for a deubiquitinating enzyme: Liquid facets is the substrate of Fat facets. Genes Dev. 16, 289–294 (2002). · DOI
  47. Nelson, K. K. & Lemmon, S. K. Suppressors of clathrin deficiency: overexpression of ubiquitin rescues lethal strains of clathrin-deficient Saccharomyces cerevisiae. Mol. Cell. Biol. 13, 521–532 (1993). · DOI
  48. Collins, B. M., McCoy, A. J., Kent, H. M., Evans, P. R. & Owen, D. J. Molecular architecture and functional model of the endocytic AP2 complex. Cell 109, 523–535 (2002). · DOI · Paper page
  49. Tebar, F., Sorkina, T., Sorkin, A., Ericsson, M. & Kirchhausen, T. Eps15 is a component of clathrin-coated pits and vesicles and is located at the rim of coated pits. J. Biol. Chem. 271, 28727–28730 (1996). · DOI
  50. Takei, K., McPherson, P. S., Schmid, S. L. & De Camilli, P. Tubular membrane invaginations coated by dynamin rings are induced by GTP-γ S in nerve terminals. Nature 374, 186–190 (1995). · DOI
  51. Riezman, H. Cell biology: the ubiquitin connection. Nature 416, 381–383 (2002). · DOI
  52. Ikeda, M., Ishida, O., Hinoi, T., Kishida, S. & Kikuchi, A. Identification and characterization of a novel protein interacting with Ral-binding protein 1, a putative effector protein of Ral. J. Biol. Chem. 273, 814–821 (1998). · DOI · Paper page
  53. Morinaka, K. et al. Epsin binds to the EH domain of POB1 and regulates receptor-mediated endocytosis. Oncogene 18, 5915–5922 (1999). · DOI
  54. Nakashima, S. et al. Small G protein Ral and its downstream molecules regulate endocytosis of EGF and insulin receptors. EMBO J. 18, 3629–3642 (1999). · DOI · Paper page
  55. Piros, E. T., Shen, L. & Huang, X. Y. Purification of an EH domain-binding protein from rat brain that modulates the gating of the rat ether-à-go-go channel. J. Biol. Chem. 274, 33677–33683 (1999). · DOI
  56. Pardo, L. A., Bruggemann, A., Camacho, J. & Stuhmer, W. Cell cycle-related changes in the conducting properties of r-eag K+ channels. J. Cell Biol. 143, 767–775 (1998). · DOI
  57. Ludwig, J., Owen, D. & Pongs, O. Carboxy-terminal domain mediates assembly of the voltage-gated rat ether-à-go-go potassium channel. EMBO J. 16, 6337–6345 (1997). · DOI
  58. Poupon, V. et al. Differential nucleocytoplasmic trafficking between the related endocytic proteins Eps15 and Eps15R. J Biol Chem 277, 8941–8948 (2002). · DOI
  59. Boronenkov, I. V., Loijens, J. C., Umeda, M. & Anderson, R. A. Phosphoinositide signaling pathways in nuclei are associated with nuclear speckles containing pre-mRNA processing factors. Mol. Biol. Cell 9, 3547–3560 (1998). · DOI
  60. Matunis, M. J., Wu, J. & Blobel, G. SUMO-1 modification and its role in targeting the Ran GTPase-activating protein, RanGAP1, to the nuclear pore complex. J. Cell Biol. 140, 499–509 (1998). · DOI
  61. Davis, C., Dube, P. & Konopka, J. B. Afr1p regulates the Saccharomyces cerevisiae α-factor receptor by a mechanism that is distinct from receptor phosphorylation and endocytosis. Genetics 148, 625–635 (1998). · DOI
  62. Misra, S., Puertollano, R., Kato, Y., Bonifacino, J. S. & Hurley, J. H. Structural basis for acidic-cluster-dileucine sorting-signal recognition by VHS domains. Nature 415, 933–937 (2002). · DOI
  63. Tebar, F., Bohlander, S. K. & Sorkin, A. Clathrin assembly lymphoid myeloid leukemia (CALM) protein: localization in endocytic-coated pits, interactions with clathrin, and the impact of overexpression on clathrin-mediated traffic. Mol. Biol. Cell 10, 2687–2702 (1999). · DOI · Paper page
  64. Legendre-Guillemin, V. et al. HIP1 and HIP12 display differential binding to F-actin, AP2, and clathrin. Identification of a novel interaction with clathrin light chain. J. Biol. Chem. 277, 19897–19904 (2002). · DOI
  65. Henry, K. R. et al. Scd5p and clathrin function are important for cortical actin organization, endocytosis, and localization of sla2p in yeast. Mol. Biol. Cell 13, 2607–2625 (2002). · DOI
  66. Engqvist-Goldstein, A. E., Kessels, M. M., Chopra, V. S., Hayden, M. R. & Drubin, D. G. An actin-binding protein of the Sla2/Huntingtin interacting protein 1 family is a novel component of clathrin-coated pits and vesicles. J. Cell Biol. 147, 1503–1518 (1999). · DOI
  67. Yang, S., Cope, M. J. & Drubin, D. G. Sla2p is associated with the yeast cortical actin cytoskeleton via redundant localization signals. Mol. Biol. Cell 10, 2265–2283 (1999). · DOI
  68. Raiborg, C., Bache, K. G., Mehlum, A., Stang, E. & Stenmark, H. Hrs recruits clathrin to early endosomes. Embo J. 20, 5008–5021 (2001). · DOI
  69. Bean, A. J. et al. Hrs-2 regulates receptor-mediated endocytosis via interactions with Eps15. J. Biol. Chem. 275, 15271–15278. (2000). · DOI
  70. Boehm, M. & Bonifacino, J. S. Adaptins: the final recount. Mol. Biol. Cell 12, 2907–2920 (2001). · DOI
  71. Boman, A. L., Zhang, C., Zhu, X. & Kahn, R. A. A family of ADP-ribosylation factor effectors that can alter membrane transport through the trans-Golgi. Mol. Biol. Cell 11, 1241–1255 (2000). · DOI · Paper page

Cited by

Sorted by citations

See all 143

Metadata

Authors
Wendland, B.
Venue
Nature Reviews Molecular Cell Biology
Published
2002-12
Volume
3
Issue
12
Pages
971-977
ISSN
  • 1471-0072
  • 1471-0080
Cited by
143
References
4
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