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Sci. STKE, 16 December 2003
[DOI: 10.1126/stke.2132003re17]

EH and UIM: Endocytosis and More
(Supplementary Information 1)

Simona Polo1,2,†, Stefano Confalonieri1,†, Anna Elisabetta Salcini1,2, and Pier Paolo Di Fiore1,2,3*

1Istituto FIRC di Oncologia Molecolare, Via Adamello 16, 20139 Milan, Italy.
2Istituto Europeo di Oncologia, Via Ripamonti 435, 20141 Milan, Italy.
3University of Milan, Medical School, 20122 Milan, Italy.
S. P. and S. C. contributed equally.

*Corresponding author. E-mail: difiore{at}ifom-firc.it

Domain Entrez-linked PDB accession number Reference
EH1 domain of mouse Eps15 1QJT (1, 2)
EH2 domain of human Eps15 in complex with the peptide PTGSSSTNPFL 1FF1 (3)
EH3 domain of human Eps15 1C07 (4)
EH domain of Pob1 1IQ3 (5)
Reps1 EH domain 1FI6 (6)
UEV domain of Tsg101 1KPP (7)
CUE domains of Vps9p and Cue2 yeast proteins 1MN3, 1OTR (8, 9)
Internal and C-terminal UBA domains of Hhr23A and of hHR23B 1IFY, 1DV0, 1P1A a (10, 11,12)
Ubiquitin interacting motif (UIM) of Vps27p and model of the UIM domain of Hrs 1O06 (13, 14)

Table 1. Known structures of EH and ubiquitin-binding domains. The table provides references and the links to the Protein Data Bank (PDB) structures in Entrez. aStructure factors deposited with PDB to be released with coordinates after publication.

References

  1. B. Whitehead, M. Tessari, H. H. Versteeg, S. van Delft, P. M. van Bergen en Henegouwen, G. W. Vuister, Sequence-specific 1H, 13C and 15N assignment of the EH1 domain of mouse Eps15. J. Biomol. NMR 12, 465-466 (1998). [CrossRef][Medline]
  2. B. Whitehead, M. Tessari, A. Carotenuto, P. M. van Bergen en Henegouwen, G. W. Vuister, The EH1 domain of Eps15 is structurally classified as a member of the S100 subclass of EF-hand-containing proteins. Biochemistry 38, 11271-11277 (1999). [CrossRef][Medline]
  3. T. de Beer, R. E. Carter, K. E. Lobel-Rice, A. Sorkin, M. Overduin, Structure and Asn-Pro-Phe binding pocket of the Eps15 homology domain. Science 281, 1357-1360 (1998). [Abstract/Free Full Text]
  4. J. L. Enmon, T. de Beer, M. Overduin, Solution structure of Eps15's third EH domain reveals coincident Phe-Trp and Asn-Pro-Phe binding sites. Biochemistry 39, 4309-4319 (2000). [CrossRef][Medline]
  5. S. Koshiba, T. Kigawa, J. Iwahara, A. Kikuchi, S. Yokoyama, Solution structure of the Eps15 homology domain of a human POB1 (partner of RalBP1). FEBS Lett. 442, 138-142 (1999). [CrossRef][Medline]
  6. S. Kim, D. N. Cullis, L. A. Feig, J. D. Baleja, Solution structure of the Reps1 EH domain and characterization of its binding to NPF target sequences. Biochemistry 40, 6776-6785 (2001). [CrossRef][Medline]
  7. O. Pornillos, S. L. Alam, R. L. Rich, D. G. Myszka, D. R. Davis, W. I. Sundquist, Structure and functional interactions of the Tsg101 UEV domain. EMBO J. 21, 2397-2406 (2002). [Abstract/Free Full Text]
  8. G. Prag, S. Misra, E. A. Jones, R. Ghirlando, B. A. Davies, B. F. Horazdovsky, J. H. Hurley, Mechanism of ubiquitin recognition by the CUE domain of Vps9p. Cell 113, 609-620 (2003). [Medline]
  9. R. S. Kang, C. M. Daniels, S. A. Francis, S. C. Shih, W. J. Salerno, L. Hicke, I. Radhakrishnan, Solution structure of a CUE-ubiquitin complex reveals a conserved mode of ubiquitin binding. Cell 113, 621-630 (2003). [Medline]
  10. T. D. Mueller, J. Feigon, Solution structures of UBA domains reveal a conserved hydrophobic surface for protein-protein interactions. J. Mol. Biol. 319, 1243-1255 (2002). [CrossRef][Medline]
  11. T. Dieckmann, E. S. Withers-Ward, M. A. Jarosinski, C. F. Liu, I. S. Chen, J. Feigon, Structure of a human DNA repair protein UBA domain that interacts with HIV-1 Vpr. Nat. Struct. Biol. 5, 1042-1047 (1998). [CrossRef][Medline]
  12. K. S. Ryu, K. J. Lee, S. H. Bae, B. K. Kim, K. A. Kim, B. S. Choi, Binding surface mapping of intra and inter domain interactions among hHR23B, ubiquitin and poly ubiquitin binding site 2 of S5a. J. Biol. Chem. 278, 36621-36627 (2003). [Abstract/Free Full Text]
  13. R. D. Fisher, B. Wang, S. L. Alam, D. S. Higginson, H. Robinson, W. I. Sundquist, C. P. Hill, Structure and ubiquitin binding of the ubiquitin interacting motif. J. Biol. Chem. 278, 28976-28984 (2003). [Abstract/Free Full Text]
  14. A. Shekhtman, D. Cowburn, A ubiquitin-interacting motif from Hrs binds to and occludes the ubiquitin surface necessary for polyubiquitination in monoubiquitinated proteins. Biochem. Biophys. Res. Commun. 296, 1222-1227 (2002). [CrossRef][Medline]

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Citation: S. Polo, S. Confalonieri, A. E. Salcini, P. P. Di Fiore, EH and UIM: Endocytosis and more. Sci. STKE 2003, re17 (2003).

© 2003 American Association for the Advancement of Science


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