Linking Ubiquitin Research to Drug Discovery

April 2015: PINK1-Parkin products

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Data supports a model in which 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). In support of further research to follow up on these exciting discoveries Ubiquigent is pleased to announce that in collaboration with UbiQ Bio BV and the University of Dundee we have added the following PINK1/Parkin signalling-related phosphorylated ubiquitins to our extensive portfolio of reagents.

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  • April 2015: PINK1-Parkin products