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Dr. Christian Johannes Gloeckner

Professor
Center for Neurodegenerative Diseases
German Centre for Neurodegenerative Diseases (Deutsches Zentrum für Neurodegenerative Erkrankungen)
Germany

Biography

Dr. Christian Johannes Gloeckner studied Biochemistry at the University of Hannover and the Hannover Medical School. He received his PhD at the Technical University of Munich in 2001. In his doctoral thesis Dr. Gloeckner studied protein-protein interactions of peroxisomal membrane proteins via the yeast two hybrid system, including the adrenoleukodystrophy-associated ABC-transporter ABCD1 (ALD). As postdoctoral Fellow (2001-2004) at the Ludwig Maximilians University Munich he focused on the development of affinity-tag combinations for systematic purification and characterization of protein complexes involved in inherited human diseases via mass spectrometry. During this time he also got sound experience in running liquid-chromatography coupled tandem mass spectrometers. Later, at the Helmholtz Zentum München (2004-2014) and the University of Tübingen (2010-2014) he was mainly focused on the functional characterization of the Parkinson’s Disease associated protein LRRK2, participating in several studies addressing LRRK2 biochemistry; among them one of the first demonstrations of LRRK2 kinase activity (2006). From 2012 to 2015 he was coordinating a consortial project aiming at the systematic analysis of the LRRK2 protein interaction network funded by the Michael J. Fox Foundation. Since 2015 he is group leader at the DZNE.

Research Interest

The workgroup focuses on the analysis of functional protein networks associated with pathogenic gene variants causing Parkinson’s Disease (PD). By systematically following the ‘guilt-by-association principle’ we aim at defining functional protein networks altered by disease to identify mutation-specific molecular pathomechanisms. Towards this goal, we are combining affinity-based purification with different methods of quantitative mass spectrometry to identify protein-protein networks and posttranslational protein modification patterns (i.e. protein phosphorylation and ubiquitination) associated with proteins mutated in familial forms of PD. Taking advantage of the multidisciplinary environment at the DZNE, the findings are subsequently validated by functional analyses in cell systems such as patient-derived induced pluripotent stem cells (iPS). Given that mutations in the LRRK2 gene are the most common reason of familial forms of PD with known genetic cause, a strong focus is laid on the systematic analysis of the gene product, the Leucine-rich repeat kinase 2 protein.

Publications

  • LRRK2 transport is regulated by its novel interacting partner Rab32. Waschbüsch D, Michels H, Strassheim S, Ossendorf E, Kessler D, Gloeckner CJ, Barnekow A. (2014). PLoS One. 9:e111632.

  • A visual review of the interactome of LRRK2: Using deep-curated molecular interactions data to represent biology. Porras P, Duesbury M, Fabregat A, Ueffing M, Orchard S, Gloeckner CJ, Hermjakob H (2015). Proteomics, 15:1390-1404

  • A structural model of the Parkinson’s Disease protein LRRK2 reveals a compact architecture involving distant inter-domain contacts Guaitoli G, Raimondi F, Gilsbach BK, Gómez-Llorente Y, Deyaert E, Renzi F, Li X, Schaffner A, Jagtap PKA, Boldt K, von Zweydorf F, Gotthardt K, Lorimer DD, Yue Z, Burgin A, Janjic N, Sattler M, Versées W, Ueffing M, Ubarretxena-Belandia I, Kortholt A and Gloeckner CJ (2016). PNAS.

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