Protein Ubiquitination in Parkinson's Disease.
Credit: Krishnan Padmanabhan, Carnegie Mellon University
Towards Elucidation of the Role of Ubiquitination in the Pathogenesis of Parkinson's Disease with Semisynthetic Ubiquitinated alpha-Synuclein.
The semisynthesis and characterization of a site specifically monoubiquitinated form of asynuclein enabled the group of Prof. H. A. Lashuel (LMNN - Laboratory of Molecular Neurobiology and Neuroproteomics), in collaboration with the group of Prof. Ashraf Brik at Ben Gurion University, to investigate the effect of ubiquitination on membrane binding, oligomerization, and fibrillogenesis. The results presented highlight the potential of applying advances in the semisynthesis of proteins to dissect the role of post-translational modifications in the pathogenesis of Parkinson's disease and development of tools that will aid in the development of diagnostic approaches to monitor the progression of the disease.
M. Hejjaoui et al., Angew. Chem. Int. Ed., 49, 1–6 (2010) - chosen as a "Hot Paper" by the Editors for its importance in a rapidly evolving field of high current interest.
Image - The painting, by Carnegie Mellon postdoc Krishnan Padmanabhan, is an image of mitral cells taking a single signal (the while line arriving from the left) and breaking it up into components, the same way a prism might break up wavelengths of light. The painting illustrates that the intrinsic differences between these neurons, allow the population of cells to represent more of the signal than each neuron may be able to do alone. (Credit: Krishnan Padmanabhan, Carnegie Mellon University)