Goto, E., Ishido, S., Sato, Y., Ohgimoto, S., Ohgimoto, K., Nagano-Fujii, M. et al. (2003) c-MIR, a human E3 ubiquitin ligase, is a functional homolog of herpesvirus proteins MIR1 and MIR2 and has similar activity. Journal of Biological Chemistry, 278, 14657-14658. doi:10.1074/jbc.M211285200

has been cited by the following article:

• TITLE: Cell-type specific regulation of MARCH1 E3 ubiquitin ligase by the anti-inflammatory cytokine IL-10

  AUTHORS: Tristan Galbas, Jacques Thibodeau

  KEYWORDS: MARCH1; Interleukin-10; MHC-II; Ubiquitin; Antigen-Presenting Cells

  JOURNAL NAME: Open Journal of Immunology, Vol.2 No.4, December 31, 2012

  ABSTRACT: Membrane-associated RING-CH-1 (MARCH1) is an E3 ubiquitin ligase which targets MHC-II, CD86 and various other molecules for degradation. It is one of the most efficient post-translational regulators of antigen presentation. MARCH1 is expressed in resting immature dendritic cells and B cells but can be induced in other cell types. While activation of most immune cells results in a reduction in MARCH1 gene expression, its anti-inflammatory properties are highlighted by its induction in response to IL-10. Here, we review what is known about the regulation of MARCH1 gene expression in response to IL-10 by various immune cells. We speculate on the role of MARCH1 ininfection, its differential expression pattern and the promise that this E3 ubiquitin ligase holds to influence immune responses and mitigate immune pathologies.