Structural basis of ubiquitin recognition by mammalian Eap45 GLUE domain (original) (raw)

Nature Structural & Molecular Biology volume 13, pages 1031–1032 (2006)Cite this article

Abstract

ESCRT-II, a complex that sorts ubiquitinated membrane proteins to lysosomes, localizes to endosomes through interaction between the Vps36 subunit's GLUE domain and phosphatidylinositides (PIs). In yeast, a ubiquitin (Ub)-interacting NZF domain is inserted in Vps36 GLUE, whereas its mammalian counterpart, Eap45 GLUE, lacks the NZF domain. In the Eap45 GLUE–Ub complex structure, Ub binds far from the proposed PI-binding site of Eap45 GLUE, suggesting their independent binding.

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Acknowledgements

This work was supported in part by the Protein 3000 project, by grants-in-aid from the Ministry of Education, Culture, Sports, Science and Technology of Japan and by the Norwegian Cancer Society, the Research Council of Norway and the Novo-Nordisk Foundation.

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Author notes

  1. Satoshi Hirano
    Present address: Biometal Science Laboratory, RIKEN SPring-8 Center, Harima Institute, Sayo, Hyogo, 679-5148, Japan

Authors and Affiliations

  1. Structural Biology Research Center, Photon Factory, Institute of Materials Structure Science, High Energy Accelerator Research Organization (KEK), Tsukuba, Ibaraki, 305–0801, Japan
    Satoshi Hirano, Nobuhiro Suzuki, Masato Kawasaki, Daniel Trambaiolo, Ryuichi Kato & Soichi Wakatsuki
  2. Department of Biochemistry, Faculty Division of the Norwegian Radium Hospital, University of Oslo, Montebello, Oslo, N-0310, Norway
    Thomas Slagsvold & Harald Stenmark

Authors

  1. Satoshi Hirano
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  2. Nobuhiro Suzuki
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  3. Thomas Slagsvold
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  4. Masato Kawasaki
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  5. Daniel Trambaiolo
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  6. Ryuichi Kato
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  7. Harald Stenmark
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  8. Soichi Wakatsuki
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Correspondence toSoichi Wakatsuki.

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Hirano, S., Suzuki, N., Slagsvold, T. et al. Structural basis of ubiquitin recognition by mammalian Eap45 GLUE domain.Nat Struct Mol Biol 13, 1031–1032 (2006). https://doi.org/10.1038/nsmb1163

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