Viral and cellular MARCH ubiquitin ligases and cancer

Xiaoli Wang, Roger A. Herr, Ted Hansen

Research output: Contribution to journalReview articlepeer-review

42 Scopus citations


Covalent conjugation of proteins with ubiquitin is one the most important post-translational modifications because it controls intracellular protein trafficking typically resulting in protein degradation. Frequently ubiquitinated proteins are targeted to the proteasome for degradation in the cytosol. However, ubiquitinated membrane bound proteins can also be targeted for endocytosis and degradation in the lysosome. Ubiquitin-dependent degradation pathways have clear cancer relevance due to their integral involvement in protein quality control, regulation of immune responses, signal transduction, and cell cycle regulation. In spite of its fundamental importance, little is known regarding how proteins are specifically identified for ubiquitin-dependent degradation. In this article we review a newly discovered family of viral and cellular ubiquitin ligases called MARCH proteins. Recent studies of MARCH proteins define new paradigms showing how ubiquitin E3 ligases determine the intracellular location and fate of proteins.

Original languageEnglish
Pages (from-to)441-450
Number of pages10
JournalSeminars in Cancer Biology
Issue number6
StatePublished - Dec 2008


  • Degradation pathways
  • Immune evasion
  • Intracellular trafficking
  • Kaposi's sarcoma-associated herpes virus
  • Ubiquitination
  • γHerpesvirus-68


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