RING domains: master builders of molecular scaffolds?

J Mol Biol. 2000 Feb 4;295(5):1103-12. doi: 10.1006/jmbi.1999.3429.

Abstract

Intense interest in the RING domain has arisen because of its widespread occurrence and involvement in human disease. Several intriguing characteristics evident from the study of this cysteine-rich, zinc-binding domain have made it difficult to establish a single defining biochemical function for RINGs. These proteins are found throughout the cell and mediate diverse cellular processes, e.g. oncogenesis, apoptosis, development and viral infection. Recent developments indicate that RING-mediated protein interactions are critical for transcriptional repression and for ubiquitination. These data are in addition to previously established functions for RINGs in RNA processing, cell-cycle control and peroxisomal biogenesis, to name a few. At first glance, there appears to be little to link such disparate actions. Collectively, these results suggest that RINGs function in formation and architecture of large protein complexes that contribute to diverse cellular processes. Here, new developments, in the context of previous results, are discussed in an attempt to establish a unifying theory for RING function.

Publication types

  • Research Support, U.S. Gov't, P.H.S.
  • Review

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Binding Sites
  • DNA-Binding Proteins / chemistry
  • DNA-Binding Proteins / metabolism
  • Humans
  • Ligases / metabolism
  • Macromolecular Substances
  • Protein Structure, Tertiary / physiology*
  • Protozoan Proteins*
  • Substrate Specificity
  • Ubiquitin-Protein Ligases
  • Ubiquitins / metabolism
  • Zinc Fingers / physiology*

Substances

  • DNA-Binding Proteins
  • KAP1 protein, Crithidia fasciculata
  • Macromolecular Substances
  • Protozoan Proteins
  • Ubiquitins
  • Ubiquitin-Protein Ligases
  • Ligases