Evans et al., Baltimore, United States. In Mol Reprod Dev, Feb 2016
UNASSIGNED: Ubiquitin C-Terminal Hydrolase L1 (UCH-L1) is thought to have multiple functions in mammalian oocytes and early embryos (e.g., Mtango et al. 2011; Sekiguchi et al. 2006); indeed, UCH-L1 is enriched in the egg cortex (Sekiguchi et al. 2006).
Ubiquitin modifications and cross-talk between proteins within these signaling cascades potentiate IFN-I expression, and inversely, a growing number of viruses are found to weaponize the ubiquitin modification system to suppress IFN-I.
Li et al., Atlanta, United States. In Transl Neurodegener, Dec 2015
The identification of mutations in mitochondrial serine/threonine kinase PINK1 or E3 ubiquitin-protein ligase parkin as the cause of autosomal recessive PD opens up new avenues for uncovering neuroprotective pathways and PD pathogenic mechanisms.
Shao et al., Nanchang, China. In Dig Dis Sci, 2012
This study identified eEF1A1 as a FAT10-specific binding protein, and when the expression of FAT10 was reduced by siRNA knockdown, this resulted in downregulation of eEF1A1 expression in hepatoma cells.
Kloetzel et al., Berlin, Germany. In Cell Mol Life Sci, 2012
FAT10 modification of the HCMV-derived antigen pp65 (FAT10-pp65) enhances the presentation of the HLA-A2-restricted pp65495-509 antigenic peptide and provide evidence that FAT10- pp65 differs from Ub-modified pp65 in using the proteasome machinery.
Groettrup et al., Konstanz, Germany. In Nat Commun, 2011
findings show how FAT10 and NUB1L dock with the 26S proteasome to initiate proteolysis; identified the 26S proteasome subunit hRpn10/S5a as the receptor for FAT10, whereas NUB1L can bind to both Rpn10 and Rpn1/S2.