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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Supplementary information
Supplementary Fig. 1
Sequence alignment of the GLUE domains. (PDF 162 kb)
Supplementary Fig. 2
Electrostatic surface potential of the phosphoinositide-binding site of GLUE domains. (PDF 67 kb)
Supplementary Fig. 3
Comparison of the ubiquitin-binding sites of mouse Eap45 and yeast Vps36. (PDF 71 kb)
Supplementary Fig. 4
Schematic drawing of ESCRT-II binding to ubiquitinated cargo and endosomal membrane. (PDF 67 kb)
Supplementary Table 1
Data collection and refinement statistics. (PDF 51 kb)
Supplementary Table 2
Sequences of QuikChange primers for Eap45 GLUE mutants. (PDF 19 kb)
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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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DOI: https://doi.org/10.1038/nsmb1163
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