Article
(Patho-)physiological relevance of PINK1-dependent ubiquitin phosphorylation.
EMBO reports - 1 Sept 2015
Fiesel Fabienne C, Ando Maya, Hudec Roman, Hill Anneliese R, Castanedes-Casey Monica, Caulfield Thomas R, Moussaud-Lamodière Elisabeth L, Stankowski Jeannette N, Bauer Peter O, Lorenzo-Betancor Oswaldo, Ferrer Isidre, Arbelo José M, Siuda Joanna, Chen Li, Dawson Valina L, Dawson Ted M, Wszolek Zbigniew K, Ross Owen A, Dickson Dennis W, Springer Wolfdieter
Abstract excerpt
Mutations in PINK1 and PARKIN cause recessive, early-onset Parkinson's disease (PD). Together, these two proteins orchestrate a protective mitophagic response that ensures the safe disposal of damaged mitochondria. The kinase PINK1 phosphorylates ubiquitin (Ub) at the conserved residue S65, in addition to modifying the E3 ubiquitin ligase Parkin. The structural and functional consequences of Ub phosphorylation...
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