A Chain of Events: Regulating Target Proteins by SUMO Polymers.
Trends Biochem Sci
; 46(2): 113-123, 2021 02.
Article
en En
| MEDLINE
| ID: mdl-33008689
ABSTRACT
Small ubiquitin-like modifiers (SUMOs) regulate virtually all nuclear processes. The fate of the target protein is determined by the architecture of the attached SUMO protein, which can be of polymeric nature. Here, we highlight the multifunctional aspects of dynamic signal transduction by SUMO polymers. The SUMO-targeted ubiquitin ligases (STUbLs) RING-finger protein 4 (RNF4) and RNF111 recognize SUMO polymers in a chain-architecture-dependent manner, leading to the formation of hybrid chains, which could enable proteasomal destruction of proteins. Recent publications have highlighted essential roles for SUMO chain disassembly by the mammalian SUMO proteases SENP6 and SENP7 and the yeast SUMO protease Ulp2. SENP6 is particularly important for centromere assembly. These recent findings demonstrate the diversity of SUMO polymer signal transduction for proteolytic and nonproteolytic purposes.
Palabras clave
Texto completo:
1
Colección:
01-internacional
Banco de datos:
MEDLINE
Asunto principal:
Polímeros
/
Proteínas Modificadoras Pequeñas Relacionadas con Ubiquitina
Límite:
Animals
Idioma:
En
Revista:
Trends Biochem Sci
Año:
2021
Tipo del documento:
Article
País de afiliación:
Países Bajos