Molecular piracy: Manipulation of the ubiquitin system by Kaposi's sarcoma-associated herpesvirus

Masahiro Fujimuro, S. Diane Hayward, Hideyoshi Yokosawa

Research output: Contribution to journalReview articlepeer-review

10 Scopus citations


Ubiquitination, one of several post-translational protein modifications, plays a key role in the regulation of cellular events, including protein degradation, signal transduction, endocytosis, protein trafficking, apoptosis and immune responses. Ubiquitin attachment at the lysine residue of cellular factors acts as a signal for endocytosis and rapid degradation by the 26S proteasome. It has recently been observed that viruses, especially oncogenic herpesviruses, utilise molecular piracy by encoding their own proteins to interfere with regulation of cell signalling. Kaposi's sarcoma- associated herpesvirus (KSHV) manipulates the ubiquitin system to facilitate cell proliferation, anti-apoptosis and evasion from immunity. In this review, we will describe the strategies used by KSHV at distinct stages of the viral life-cycle to control the ubiquitin system and promote oncogenesis and viral persistence.

Original languageEnglish (US)
Pages (from-to)405-422
Number of pages18
JournalReviews in Medical Virology
Issue number6
StatePublished - Nov 2007

ASJC Scopus subject areas

  • Virology
  • Infectious Diseases


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