The Ubiquitin-Proteasome System and F-box Proteins in Pathogenic Fungi
Mycobiology
;
: 243-248, 2011.
Article
in English
| 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.
Full text:
Available
Index:
WPRIM (Western Pacific)
Main subject:
Saccharomyces cerevisiae
/
Substrate Specificity
/
Yeasts
/
Cryptococcus neoformans
/
Ubiquitin
/
Ubiquitin-Protein Ligases
/
F-Box Proteins
/
Proteasome Endopeptidase Complex
/
Fungi
/
Ligases
Type of study:
Prognostic study
Limits:
Humans
Language:
English
Journal:
Mycobiology
Year:
2011
Type:
Article
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