The Ubiquitin-Proteasome System and F-box Proteins in Pathogenic Fungi.
- Author:
Tong Bao LIU
1
;
Chaoyang XUE
Author Information
1. Public Health Research Institute, University of Medicine and Dentistry of New Jersey, Newark, NJ 07103, USA. xuech@umdnj.edu
- Publication Type:Review
- Keywords:
Cryptococcus neoformans;
E3 ligase;
F-box;
Fungi;
Virulence
- MeSH:
Cryptococcus neoformans;
F-Box Proteins;
Fungi;
Humans;
Ligases;
Proteasome Endopeptidase Complex;
Saccharomyces cerevisiae;
Substrate Specificity;
Ubiquitin;
Ubiquitin-Protein Ligases;
Yeasts
- From:Mycobiology
2011;39(4):243-248
- CountryRepublic of Korea
- Language:English
-
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.
