The lore of the RINGs: substrate recognition and catalysis by ubiquitin ligases.
Trends Cell Biol
; 10(10): 429-39, 2000 Oct.
Article
em En
| MEDLINE
| ID: mdl-10998601
ABSTRACT
Recently, many new examples of E3 ubiquitin ligases or E3 enzymes have been found to regulate a host of cellular processes. These E3 enzymes direct the formation of multiubiquitin chains on specific protein substrates, and - typically - the subsequent destruction of those proteins. We discuss how the modular architecture of E3 enzymes connects one of two distinct classes of catalytic domains to a wide range of substrate-binding domains. In one catalytic class, a HECT domain transfers ubiquitin directly to substrate bound to a non-catalytic domain. Members of the other catalytic class, found in the SCF, VBC and APC complexes, use a RING finger domain to facilitate ubiquitylation. The separable substrate-recognition domains of E3 enzymes provides a flexible means of linking a conserved ubiquitylation function to potentially thousands of ubiquitylated substrates in eukaryotic cells.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Ligases
Limite:
Animals
/
Humans
Idioma:
En
Revista:
Trends Cell Biol
Ano de publicação:
2000
Tipo de documento:
Article
País de afiliação:
Estados Unidos