Protein–protein interactions regulate Ubl conjugation

Protein–protein interactions regulate Ubl conjugation The ubiquitin-like proteins (Ubls) can be covalently linked to target proteins to provide a critical signal in diverse cellular processes. Members of the Ubl family include ubiquitin itself and a growing number of homologs such as SUMO, Nedd8, ISG15 and Atg8. The enzymatic mechanism of Ubl conjugation involves an E1, E2, E3 cascade of enzymes that is well conserved between the Ubls. In the past two years, novel structural details of Ubl conjugation were uncovered through analysis of protein–protein complexes. This has given insight in activation of E1, the role of the target lysine in E2-dependent catalysis, the role of noncovalent Ubl binding in Ubl chain formation and the importance of dimerization of Ring-type E3 ligases. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Current Opinion in Structural Biology Elsevier

Protein–protein interactions regulate Ubl conjugation

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Publisher
Elsevier
Copyright
Copyright © 2007 Elsevier Ltd
ISSN
0959-440x
D.O.I.
10.1016/j.sbi.2007.09.001
Publisher site
See Article on Publisher Site

Abstract

The ubiquitin-like proteins (Ubls) can be covalently linked to target proteins to provide a critical signal in diverse cellular processes. Members of the Ubl family include ubiquitin itself and a growing number of homologs such as SUMO, Nedd8, ISG15 and Atg8. The enzymatic mechanism of Ubl conjugation involves an E1, E2, E3 cascade of enzymes that is well conserved between the Ubls. In the past two years, novel structural details of Ubl conjugation were uncovered through analysis of protein–protein complexes. This has given insight in activation of E1, the role of the target lysine in E2-dependent catalysis, the role of noncovalent Ubl binding in Ubl chain formation and the importance of dimerization of Ring-type E3 ligases.

Journal

Current Opinion in Structural BiologyElsevier

Published: Dec 1, 2007

References

  • Structural mechanisms underlying posttranslational modification by ubiquitin-like proteins
    Dye, B.T.; Schulman, B.A.
  • Mechanism and function of deubiquitinating enzymes
    Amerik, A.Y.; Hochstrasser, M.
  • Modification of proteins by ubiquitin and ubiquitin-like proteins
    Kerscher, O.; Felberbaum, R.; Hochstrasser, M.
  • Structures of the SUMO E1 provide mechanistic insights into SUMO activation and E2 recruitment to E1
    Lois, L.M.; Lima, C.D.
  • Structure and analysis of a complex between SUMO and Ubc9 illustrates features of a conserved E2-Ubl interaction
    Capili, A.D.; Lima, C.D.
  • Noncovalent interaction between Ubc9 and SUMO promotes SUMO chain formation
    Knipscheer, P.; van Dijk, W.J.; Olsen, J.V.; Mann, M.; Sixma, T.K.
  • Structure and E3-ligase activity of the Ring-Ring complex of polycomb proteins Bmi1 and Ring1b
    Buchwald, G.; van der Stoop, P.; Weichenrieder, O.; Perrakis, A.; van Lohuizen, M.; Sixma, T.K.
  • Solution structure of the Hdm2 C2H2C4 RING, a domain critical for ubiquitination of p53
    Kostic, M.; Matt, T.; Martinez-Yamout, M.A.; Dyson, H.J.; Wright, P.E.
  • The Mdm2 RING domain C-terminus is required for supramolecular assembly and ubiquitin ligase activity
    Poyurovsky, M.V.; Priest, C.; Kentsis, A.; Borden, K.L.; Pan, Z.Q.; Pavletich, N.; Prives, C.

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