Mycobiology

  • 제39권4호
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  • Pages.243-248
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  • 2011
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  • 1229-8093(pISSN)
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  • 2092-9323(eISSN)
한국균학회 (The Korean Society of Mycology)
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The Ubiquitin-Proteasome System and F-box Proteins in Pathogenic Fungi

  • Liu, Tong-Bao (Public Health Research Institute, University of Medicine and Dentistry of New Jersey) ;
  • Xue, Chaoyang (Public Health Research Institute, University of Medicine and Dentistry of New Jersey)
  • 투고 : 2011.11.05
  • 심사 : 2011.11.07
  • 발행 : 2011.12.31
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초록

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.

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