29 April 2015
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 we have thus developed these new reagents. For more info or to order: