Structural mechanisms underlying posttranslational modification by ubiquitin-like proteins

Annu Rev Biophys Biomol Struct. 2007;36:131-50. doi: 10.1146/annurev.biophys.36.040306.132820.

Abstract

Covalent attachment of ubiquitin-like proteins (Ubls) is a predominant mechanism for regulating protein function in eukaryotes. Several structurally related Ubls, such as ubiquitin, SUMO, NEDD8, and ISG15, modify a vast number of proteins, altering their functions in a variety of ways. Ubl modifications can affect the target's half-life, subcellular localization, enzymatic activity, or ability to interact with protein or DNA partners. Generally, these diverse Ubls are covalently attached via their C termini to their targets by parallel, but specific, cascades involving three classes of enzymes known as E1, E2, and E3. Structures are now available for many protein complexes in E1-E2-E3 cascades, revealing a series of modular building blocks and providing mechanistic insights into their functions.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Biophysics / methods
  • Gene Expression Regulation*
  • Humans
  • Models, Chemical
  • Molecular Conformation
  • Protein Conformation
  • Protein Processing, Post-Translational
  • Proteins / chemistry*
  • Ubiquitin / chemistry*
  • Ubiquitin-Activating Enzymes / chemistry*

Substances

  • Proteins
  • Ubiquitin
  • Ubiquitin-Activating Enzymes