SUMO modification of the ubiquitin-conjugating enzyme E2-25K

Nature Structural and Molecular Biology

Volumn 12, Issue 3, 2005, Pages 264-269

  Pichler, Andrea ^a,c   Knipscheer, Puck ^b   Oberhofer, Edith ^c   Van Dijk, Willem J ^b   Körner, Roman ^c   Olsen, Jesper Velgaard ^d   Jentsch, Stefan ^c   Melchior, Frauke ^a,c   Sixma, Titia K ^b  

^a UNIVERSITY OF GÖTTINGEN   (Germany)

^b NETHERLANDS CANCER INSTITUTE   (Netherlands)

^c MAX PLANCK INSTITUTE OF BIOCHEMISTRY   (Germany)

^d UNIVERSITY OF SOUTHERN DENMARK   (Denmark)

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN UBC9; SUMO PROTEIN; THIOESTER; UBIQUITIN CONJUGATING ENZYME; UBIQUITIN CONJUGATING ENZYME E2 25K; UNCLASSIFIED DRUG; HIP2 PROTEIN, HUMAN; SUMO 1 PROTEIN;

ALPHA HELIX; AMINO TERMINAL SEQUENCE; ARTICLE; BINDING SITE; CONTROLLED STUDY; CRYSTAL STRUCTURE; HUMAN; HUMAN CELL; IN VITRO STUDY; MOLECULAR MECHANICS; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN FUNCTION; PROTEIN INTERACTION; PROTEIN MODIFICATION; PROTEIN PROCESSING; PROTEIN SECONDARY STRUCTURE; PROTEIN TARGETING; AMINO ACID SEQUENCE; CONSENSUS SEQUENCE; CRYSTALLIZATION; HELA CELL; METABOLISM; MOLECULAR GENETICS; PHYSIOLOGY;

AMINO ACID SEQUENCE; CONSENSUS SEQUENCE; CRYSTALLIZATION; HELA CELLS; HUMANS; MOLECULAR SEQUENCE DATA; PROTEIN INTERACTION MAPPING; PROTEIN PROCESSING, POST-TRANSLATIONAL; PROTEIN STRUCTURE, SECONDARY; SUMO-1 PROTEIN; UBIQUITIN-CONJUGATING ENZYMES;

EID: 17844401751     PISSN: 15459993     EISSN: 15459985     Source Type: Journal    
DOI: 10.1038/nsmb903     Document Type: Article

References (38)

1. Pickart, C.M. Mechanisms underlying ubiquitination. Annu. Rev. Biochem. 70, 503-533 (2001).
2. Passmore, L.A. & Barford, D. Getting into position: the catalytic mechanisms of protein ubiquitylation. Biochem. J. 379, 513-525 (2004).
3. Pichler, A. & Melchior, F. SUMO E3 ligases. In SUMOylation. Molecular Biology and Biochemistry (ed. Van Wilson, G.) (Horizon Press, Norwich, UK, 2004).
4. Johnson, E.S. Protein modification by SUMO. Annu. Rev. Biochem. 73, 355-382 (2004).
5. Macauley, M.S. et al. Structural and dynamic independence of isopeptide-linked RanGAP1 and SUMO-1. J. Biol. Chem. 279, 49131-49137 (2004).
6. Chen, Z. & Pickart, C.M. A 25-kilodalton ubiquitin carrier protein (E2) catalyzes multiubiquitin chain synthesis via lysine 48 of ubiquitin. J. Biol. Chem. 265, 21835-21842 (1990).
7. Song, S. et al. Essential role of E2-25K/Hip-2 in mediating amyloid-β neurotoxicity. Mol. Cell 12, 553-563 (2003).
8. Kalchman, M.A. et al. Huntingtin is ubiquitinated and interacts with a specific ubiquitin-conjugating enzyme. J. Biol. Chem. 271, 19385-19394 (1996).
9. Lelouard, H. et al. Dendritic cell aggresome-like induced structures are dedicated areas for ubiquitination and storage of newly synthesized defective proteins. J. Cell Biol. 164, 667-675 (2004).
10. Girdwood, D. et al. P300 transcriptional repression is mediated by SUMO modification. Mol. Cell 11, 1043-1054 (2003).
11. Hardeland, U., Steinacher, R., Jiricny, J. & Schar, P. Modification of the human thymine-DNA glycosylase by ubiquitin-like proteins facilitates enzymatic turnover. EMBO J. 21, 1456-1464 (2002).
12. Hoege, C., Pfander, B., Moldovan, G.L., Pyrowolakis, G. & Jentsch, S. RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO. Nature 419, 135-141 (2002).
13. Huang, T.T., Wuerzberger-Davis, S.M., Wu, Z.H. & Miyamoto, S. Sequential modification of NEMO/IKKγ by SUMO-1 and ubiquitin mediates NF-κB activation by genotoxic stress. Cell 115, 565-576 (2003).
14. Haldeman, M.T., Xia, G., Kasperek, E.M. & Pickart, C.M. Structure and function of ubiquitin conjugating enzyme E2-25K: the tail is a core-dependent activity element. Biochemistry 36, 10526-10537 (1997).
15. Hamilton, K.S. et al. Structure of a conjugating enzyme-ubiquitin thiolester intermediate reveals a novel role for the ubiquitin tail. Structure 9, 897-904 (2001).
16. Cook, W.J., Jeffrey, L.C., Kasperek, E. & Pickart, C.M. Structure of tetraubiquitin shows how multiubiquitin chains can be formed. J. Mol. Biol. 236, 601-609 (1994).
17. Phillips, C.L., Thrower, J., Pickart, C.M. & Hill, C.P. Structure of a new crystal form of tetraubiquitin. Acta Crystallogr. D 57, 341-344 (2001).
18. 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).
19. Mossessova, E. & Lima, C.D. Ulp1-SUMO crystal structure and genetic analysis reveal conserved interactions and a regulatory element essential for cell growth in yeast. Mol. Cell 5, 865-876 (2000).
20. Walden, H. et al. The structure of the APPBP1-UBA3-NEDD8-ATP complex reveals the basis for selective ubiquitin-like protein activation by an E1. Mol. Cell 12, 1427-1437 (2003).
21. Sullivan, M.L. & Vierstra, R.D. Cloning of a 16-kDa ubiquitin carrier protein from wheat and Arabidopsis thaliana. Identification of functional domains by in vitro mutagenesis. J. Biol. Chem. 266, 23878-23885 (1991).
22. Bencsath, K.P., Podgorski, M.S., Pagala, V.R., Slaughter, C.A. & Schulman, B.A. Identification of a multifunctional binding site on Ubc9p required for Smt3p conjugation. J. Biol. Chem. 277, 47938-47945 (2002).
23. Huang, D.T. et al. A unique E1-E2 interaction required for optimal conjugation of the ubiquitin-like protein NEDD8. Nat. Struct. Mol. Biol. 11, 927-935 (2004).
24. Sampson, D.A., Wang, M. & Matunis, M.J. The small ubiquitin-like modifier-1 (SUMO-1) consensus sequence mediates Ubc9 binding and is essential for SUMO-1 modification. J. Biol. Chem. 276, 21664-21669 (2001).
25. Bernier-Villamor, V., Sampson, D.A., Matunis, M.J. & Lima, C.D. Structural basis for E2-mediated SUMO conjugation revealed by a complex between ubiquitin-conjugating enzyme Ubc9 and RanGAP1. Cell 108, 345-356 (2002).
26. Lin, D. et al. Identification of a substrate recognition site on Ubc9. J. Biol. Chem. 277, 21740-21748 (2002).
27. Huang, L. et al. Structure of an E6AP-UbcH7 complex: insights into ubiquitination by the E2-E3 enzyme cascade. Science 286, 1321-1326 (1999).
28. Cope, G.A. & Deshaies, R.J. COP9 signalosome: a multifunctional regulator of SCF and other cullin-based ubiquitin ligases. Cell 114, 663-671 (2003).
29. Wolf, D.A., Zhou, C. & Wee, S. The COP9 signalosome: an assembly and maintenance platform for cullin ubiquitin ligases? Nat. Cell Biol. 5, 1029-1033 (2003).
30. Mahajan, R., Delphin, C., Guan, T., Gerace, L. & Melchior, F. A small ubiquitin-related polypeptide involved in targeting RanGAP1 to nuclear pore complex protein RanBP2. Cell 88, 97-107 (1997).
31. Pichler, A., Gast, A., Seeler, J.S., Dejean, A. & Melchior, F. The nucleoporin RanBP2 has SUMO1 E3 ligase activity. Cell 108, 109-120 (2002).
32. Haldeman, M.T., Finley, D. & Pickart, C.M. Dynamics of ubiquitin conjugation during erythroid differentiation in vitro. J. Biol. Chem. 270, 9507-9516 (1995).
33. Shevchenko, A., Wilm, M., Vorm, O. & Mann, M. Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels. Anal. Chem. 68, 850-858 (1996).
34. Gobom, J., Nordhoff, E., Mirgorodskaya, E., Ekman, R. & Roepstorff, P. Sample purification and preparation technique based on nano-scale reversed-phase columns for the sensitive analysis of complex peptide mixtures by matrix-assisted laser desorption/ionization mass spectrometry. J. Mass Spectrom. 34, 105-116 (1999).
35. Collaborative Computational Project 4. The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D 50, 760-763 (1994).
36. Perrakis, A., Morris, R. & Lamzin, V.S. Automated protein model building combined with iterative structure refinement. Nat. Struct. Biol. 6, 458-463 (1999).
37. Jones, T.A., Zou, J.Y., Cowan, S.W. & Kjeldgaard. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A 47, 110-119 (1991).
38. Pickart, C.M. & Vella, A.T. Levels of active ubiquitin carrier proteins decline during erythroid maturation. J. Biol. Chem. 263, 12028-12035 (1988).