Cover Picture: Alpha‐Synuclein Binds to the Inner Membrane of Mitochondria in an α‐Helical Conformation (ChemBioChem 17/2014). Issue 17 (24th November 2014)

• Record Type: Journal Article
• Authors: Robotta, Marta; Gerding, Hanne R.; Vogel, Antonia; Hauser, Karin; Schildknecht, Stefan; Karreman, Christiaan; Leist, Marcel; Subramaniam, Vinod; Drescher, Malte
• Is Part Of: Chembiochem. Volume 15:Issue 17(2014)
• Page Start: 2473
• Page End: 2473
• Publication Date: 2014-11-24
• Subjects: Biochemistry -- Periodicals; Molecular biology -- Periodicals; Pharmaceutical chemistry -- Periodicals; 572
• DOI: 10.1002/cbic.201490058
• Languages: English
• ISSNs: 1439-4227

Abstract

<abstract abstract-type="graphical" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p> <bold>The cover picture shows</bold> an artist's view of how alpha‐Synuclein binds to mitochondria. alpha‐Synuclein is an intrinsically disordered protein that adapts a variety of different conformations upon macromolecular interactions and is therefore also called a protein chameleon. Many intrinsically disordered proteins are involved in neurodegenerative diseases and so is alpha‐Synuclein. Although its physiological function is still to be determined, alpha‐Synuclein is the main protein component of Lewy bodies, a hallmark of Parkinson's disease. M. Drescher et al. <ext-link ext-link-type="doi" xlink:type="simple" xmlns:xlink="http://www.w3.org/1999/xlink">(see p. 2499 ff)</ext-link> used paramagnetic labels, here represented by horseshoe magnets, to determine distance constraints by electron paramagnetic resonance spectroscopy. The advantage of EPR spectroscopy in combination with site‐directed spin‐labeling—that it is virtually background free—is of utmost importance for making measurements in complex environments, like the membranes of mitochondria. The results presented here suggest that alpha‐Synuclein exhibits an α‐helical conformation upon binding to the inner membrane of mitochondria.<boxed-text content-type="graphic" position="anchor" orientation="portrait"><graphic position="anchor" mimetype="image" xlink:href="ark:/27927/pgh2cpvhkk2" orientation="portrait" xlink:type="simple" xmlns:xlink="http://www.w3.org/1999/xlink" /></boxed-text></p> </abstract>