Modification of the inflammatory mediator LRRFIP2 by the ubiquitin-like protein FAT10 inhibits its activity during cellular response to LPS.

@article{Buchsbaum2012ModificationOT,
  title={Modification of the inflammatory mediator LRRFIP2 by the ubiquitin-like protein FAT10 inhibits its activity during cellular response to LPS.},
  author={S. Buchsbaum and B. Bercovich and T. Ziv and A. Ciechanover},
  journal={Biochemical and biophysical research communications},
  year={2012},
  volume={428 1},
  pages={
          11-6
        }
}
FAT10 is a ubiquitin-like protein made of two tandem, head-to-tail, ubiquitin domains. It is known to covalently modify proteins in a mechanism similar, though not identical, to that of other ubiquitin-like proteins. The lack of known physiological substrates covalently conjugated by the protein made it difficult to unravel its biological functions. Here we identify two proteins that are covalently modified by FAT10, the inflammatory mediator LRRFIP2 and the endoplasmic reticulum membrane… Expand
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