Polyubiquitin chain-dependent protein degradation in TRIM30 cytoplasmic bodies
Experimental & Molecular Medicine
; : e159-2015.
Article
em Ko
| WPRIM
| ID: wpr-147141
Biblioteca responsável:
WPRO
ABSTRACT
Viral infection induces numerous tripartite motif (TRIM) proteins to control antiviral immune signaling and viral replication. Particularly, SPRY-containing TRIM proteins are found only in vertebrates and they control target protein degradation by their RING-finger and SPRY domains, and proper cytoplasmic localization. To understand TRIM30 function, we analyzed its localization pattern and putative roles of its RING-finger and SPRY domains. We found that TRIM30 is located in actin-mediated cytoplasmic bodies and produces colocalized ubiquitin chains in SPRY domain- and RING-finger domain-dependent ways that are degraded by autophagy and the proteasome. These results suggest a TRIM protein-dependent degradation mechanism by cytoplasmic body formation with actin networks.
Texto completo:
1
Base de dados:
WPRIM
Assunto principal:
Autofagia
/
Dados de Sequência Molecular
/
Linhagem Celular
/
Corpos de Inclusão
/
Sequência de Aminoácidos
/
Transporte Proteico
/
Poliubiquitina
/
Complexo de Endopeptidases do Proteassoma
/
Peptídeos e Proteínas de Sinalização Intracelular
/
Domínios RING Finger
Limite:
Animals
Idioma:
Ko
Revista:
Experimental & Molecular Medicine
Ano de publicação:
2015
Tipo de documento:
Article