Structural and Functional Impact of Parkinson Disease‐Associated Mutations in the E3 Ubiquitin Ligase Parkin. Issue 8 (3rd June 2015)

• Record Type: Journal Article
• Authors: Fiesel, Fabienne C.; Caulfield, Thomas R.; Moussaud‐Lamodière, Elisabeth L.; Ogaki, Kotaro; Dourado, Daniel F.A.R.; Flores, Samuel C.; Ross, Owen A.; Springer, Wolfdieter
• Is Part Of: Human mutation. Volume 36:Issue 8(2015:Aug.)
• Page Start: 774
• Page End: 786
• Publication Date: 2015-06-03
• Subjects: Human chromosome abnormalities -- Periodicals; Mutation (Biology) -- Periodicals; 616.04205
• DOI: 10.1002/humu.22808
• Languages: English
• ISSNs: 1059-7794

Abstract

<abstract abstract-type="graphical" xml:lang="en" id="humu22808-abs-0001"> <title> <x xml:space="preserve">Abstract</x> </title> <p>Fiesel et al., provides a structure‐function analysis of human PARK2 mutations and pathogenic PD mechanisms. The crystalline structure in the front shows the 'closed', auto‐inhibited conformation of the E3 ubiquitin ligase Parkin. Upon activation by PINK1, Parkin undergoes major structural rearrangements in order to gain enzymatic activity. The functional data in the monochrome background are obtained from cell‐based imaging of the Parkin mutants. Activation and enzymatic activity of Parkin is coupled to its translocation from the cytosol onto damaged mitochondria. <graphic position="anchor" mimetype="image" xlink:href="ark:/27927/pgj296tvwd3" orientation="portrait" xlink:type="simple" xmlns:xlink="http://www.w3.org/1999/xlink" /></p> </abstract>