The small ubiquitin-like modifier (SUMO) protein is an ubiquitin-like (UBL) protein that is highly dynamic and can reversibly target lysine residues on a wide range of proteins involved in several essential cellular events including protein translocation and degradation.Quantitative SUMO proteomics identifies PIAS1 substrates involved in cell migration and motility.
The current investigation highlights the role of PIAS1 downregulation in the evolution of graft rejection and potentiates this gene as a predictive marker for transplant fate.
PIAS1expression of PIAS1 gene was increased in patients with MS compared to healthy subjects; also there was a significant correlation between the expression of PIAS1 and PIAS2 genes with disease severity of multiple sclerosis
PIAS1 as a key regulator of Epstein-Barr Virus lytic replication. PIAS1 acts as an inhibitor for transcription factors involved in lytic gene expression.
Rad18 independently of its ubiquitin ligase activity promotes DNA polymerase eta SUMOylation by facilitating its interaction with its SUMO ligase PIAS1 and is required for DNA polymerase eta function at difficult to replicate loci.
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