The discovery that ubiquitin itself can be modified through phosphorylation by the kinase PINK1 provides a major breakthrough linking the two most important signalling pathways in cells; phosphorylation and ubiquitylation. Parkin and PINK1, the two main proteins associated with Parkinson’s Disease (PD) comprise a mitochondrial quality control pathway that promotes neuronal survival through autophagy of damaged mitochondria in a process known as mitophagy. The accumulation of PINK1 on depolarised or damaged mitochondria leads to the activation and translocation of Parkin to the outer mitochondrial membrane. Phosphorylation of Parkin by PINK1 at Ser65 located in its Ubl domain markedly increases the E3 ligase activity of Parkin resulting in ubiquitylation of proteins on the outer mitochondrial membrane, triggering selective mitophagy.

With its UbiQ-Syn technology and in close cooperation with Ubiquigent and the MRC Protein Phosphorylation and Ubiquitylation Unit (University of Dundee), UbiQ has developed a set of phospho-ubiquitin mutants, all identified in cells by proteomics These offer the opportunity to investigate the role and function of phosphorylated ubiquitin.

UbiQ-089: Ub pSer65

UbiQ-113: Ub pSer57

UbiQ-091: Biotin-Ahx-Ub pSer65

UbiQ-092: Biotin-Ahx-Ub pThr7

UbiQ-093: Biotin-Ahx-Ub pThr12

UbiQ-094: Biotin-Ahx-Ub pSer57

UbiQ-095: Biotin-Ahx-Ub pTyr59

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