TRIM family: Pleiotropy and diversification through homomultimer and heteromultimer formation.
IUBMB Life
; 64(1): 64-71, 2012 Jan.
Article
en En
| MEDLINE
| ID: mdl-22131136
ABSTRACT
The TRIM family is composed of multidomain ubiquitin E3 ligases characterized by the presence of the N-terminal tripartite motif (RING, B-boxes, and coiled coil). TRIM proteins transfer the ubiquitin moiety to specific substrates but are also involved in ubiquitin-like modifications, in particular SUMOylation and ISGylation. The TRIM family members are involved in a plethora of biological and physiological processes and, when altered, are implicated in many pathological conditions. Growing evidence indicates the pleiotropic effect of several TRIM genes, each of which might be connected to very diverse cellular processes. As a way to reconcile a single family member with several functions, we propose that structural features, that is, their ability to homo- and hetero-di(multi)merize, can increase and diversify TRIM ubiquitin E3 ligase capability.
Texto completo:
1
Colección:
01-internacional
Banco de datos:
MEDLINE
Asunto principal:
Ubiquitina-Proteína Ligasas
/
Multimerización de Proteína
Límite:
Animals
/
Humans
Idioma:
En
Revista:
IUBMB Life
Asunto de la revista:
BIOLOGIA MOLECULAR
/
BIOQUIMICA
Año:
2012
Tipo del documento:
Article
País de afiliación:
Italia