IndraLab
Statements
sparser
"The association of ISG15 with USP18 interrupts the interaction of USP18 with S-phase kinase-associated protein 2 (SKP2), inhibiting the proteasomal degradation of USP18, which is essential for negative feedback regulation of IFN signaling and prevention of autoinflammation xref , xref ."
sparser
"Several studies have reported that SAMHD1 interacts with cyclin/CDK complexes [ xref ], USP18 and S-phase kinase-associated protein 2 [ xref , xref ], which are involved in the regulation of cell proliferation [ xref , xref ] and SAMHD1 is also recruited to DNA repair foci in response to DNA damage [ xref ]."
sparser
"While these data do not rule out the possibility that indirect interactions between ISG15 (via Trp123) and an unknown partner are responsible for USP18 stability, which may be consistent with previous reports showing that ISG15 can abrogate the USP18‐SKP2 complex and rescue USP18 from proteasomal degradation independently of its ability to bind USP18 [ xref ]."
reach
"Although this is in line with the view that only a small fraction of the total pool of a given protein is ISGylated 26, we inferred that low levels of SKP2 ISGylation is unlikely to account neither for the disruption of the USP18 and SKP2 complex nor for the reduction of SKP2 (47kDa) observed upon enforced ISG15 expression."