Linking Ubiquitin Research to Drug Discovery

April 2015: Phospho-Ubiquitin products

Posted in Resource categoriesNewsletters and Articles.
Attachment: 1 Publication

Several variants of phosphorylated ubiquitin – with as yet undefined functions – have been reported in the literature. Phosphoproteomic studies have identified the presence of phosphorylated peptides demonstrating homology to proteins of the Ubiquitin Proteasome Pathway (UPP) including ubiquitin, ubiquitin like modifiers and proteins containing ubiquitin binding domains (Bennetzen et al., 2010; Bian et al., 2014; Moritz et al., 2010; Sharma et al., 2014).

Recent data has shown that the optimal activation of Parkin is regulated by a dual mechanism requiring both phosphorylation of its Ubl domain at Ser65 and the binding to Parkin of ubiquitin phosphorylated at Ser65. Critically Ser65 phosphorylation of both Parkin and ubiquitin is regulated by the kinase PINK1 (Kane et al., 2014; Kazlauskaite et al., 2014; Koyano et al., 2014).

  • April 2015: Phospho-Ubiquitin products