The Ubiquitin-Proteasome System and F-box Proteins in Pathogenic Fungi
Mycobiology
;
: 243-248, 2011.
Artículo
en Inglés
| WPRIM
| ID: wpr-729511
ABSTRACT
The ubiquitin-proteasome system is one of the major protein turnover mechanisms that plays important roles in the regulation of a variety of cellular functions. It is composed of E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3 ubiquitin ligases that transfer ubiquitin to the substrates that are subjected to degradation in the 26S proteasome. The Skp1, Cullin, F-box protein (SCF) E3 ligases are the largest E3 gene family, in which the F-box protein is the key component to determine substrate specificity. Although the SCF E3 ligase and its F-box proteins have been extensively studied in the model yeast Saccharomyces cerevisiae, only limited studies have been reported on the role of F-box proteins in other fungi. Recently, a number of studies revealed that F-box proteins are required for fungal pathogenicity. In this communication, we review the current understanding of F-box proteins in pathogenic fungi.
Texto completo:
Disponible
Índice:
WPRIM (Pacífico Occidental)
Asunto principal:
Saccharomyces cerevisiae
/
Especificidad por Sustrato
/
Levaduras
/
Cryptococcus neoformans
/
Ubiquitina
/
Ubiquitina-Proteína Ligasas
/
Proteínas F-Box
/
Complejo de la Endopetidasa Proteasomal
/
Hongos
/
Ligasas
Tipo de estudio:
Estudio pronóstico
Límite:
Humanos
Idioma:
Inglés
Revista:
Mycobiology
Año:
2011
Tipo del documento:
Artículo
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