Ueffing Lab

Molecular Biology of Retinal Degenerations

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Christian Johannes Gloeckner

SurnameGloeckner
First nameChristian Johannes
NationalityGerman
Present position and titleGroup leader, DZNE, PD Dr. rer. nat.

Business address

Deutsches Zentrum für Neurodegenerative Erkrankungen e.V. (DZNE)
University of Tübingen
Otfried-Müller-Str. 23
D-72076 Tübingen,
Germany

Phone: +49 (0)7071 9254-400
Fax: +49 (0)7071 9254-153
E-mail: christian-johannes.gloeckner[at]guest.uni-tuebingen.de

External Website: DZNE [german version] [english version]

Academic Education

Year Degree University Field of study
2017 Habilitation University of Tübingen, Faculty of Medicine Molecular Neuroscience
2001 Dr. rer nat Technical University of Munich Biochemistry
1997 Diploma University of Hannover Biochemistry

Professional Experience

Period Institution Position Discipline
2015 - present Deutsches Zentrum für Neurodegenerative Erkrankungen (DZNE) Group Leader Mass spectrometry, Neuroproteomics, LRRK2 biology
2010 - present Medical Proteome Center, Institute for Ophthalmic Research, Eberhard-Karls Universität Tübingen Group Leader Mass spectrometry, anaylsis of protein complexes in neurodegenerative diseases, LRRK2 biology
2004 - 2014 Department of Protein Science, Helmholtz-Zentrum München Staff Scientist Mass spectrometry, proteomics, analoysis of disease-associated protein complexes, LRRK2 biology
2001 - 2004 Ludwig Maximilians University Postdoctoral fellow Proteomics, Interactomics

Awards

2011LEAPS Award: "Analysis of LRRK2 protein complexes and pathway modelling (Michael J. fox Foundation)

Additional information

2010 - presentMember of the LRRK2 Biological Consortium (The Michael J. Fox Foundation for Parkinson’s Research)
2002 - presentMember, German Society for Proteome Research (DGPF)
2001Doctoral thesis ranked with “summa cum laude”, Technical University of Munich

Memberships and Functions in Scientific Societies

  • German Society for Proteome Research (DGPF)

Selected Publications

  1. Deyaert E, Wauters L, Guaitoli G, Konijnenberg A, Leemans M, Terheyden S, Petrovic A, Gallardo R, Nederveen-Schippers LM, Athanasopoulos PS, Pots H, Van Haastert PJM, Sobott F, Gloeckner CJ, Efremov R, Kortholt A, and Versees W (2017). A homologue of the Parkinson's disease-associated protein LRRK2 undergoes a monomer-dimer transition during GTP turnover. Nat Commun. 8:1008.
  2. Guaitoli G, Raimondi F, Gilsbach BK, Gomez-Llorente Y, Deyaert E, Renzi F, Li X, Schaffner A, Jagtap PK, Boldt K, von Zweydorf F, Gotthardt K, Lorimer DD, Yue Z, Burgin A, Janjic N, Sattler M, Versees W, Ueffing M, Ubarretxena-Belandia I, Kortholt A, and Gloeckner CJ (2016). Structural model of the dimeric Parkinson's protein LRRK2 reveals a compact architecture involving distant interdomain contacts. Proc. Natl Acad. Sci. U S A. 113:E4357-66
  3. Porras P, Duesbury M, Fabregat A, Ueffing M, Orchard S, Gloeckner CJ, Hermjakob H (2015). A visual review of the interactome of LRRK2: Using deep-curated molecular interactions data to represent biology. Proteomics 15, 1390-1404
  4. Waschbüsch D, Michels H, Strassheim S, Ossendorf E, Kessler D, Gloeckner CJ, Barnekow A. (2014). LRRK2 transport is regulated by its novel interacting partner Rab32. PLoS One. 9:e111632.                   
    Piccoli G, Onofri F, Cirnaru MD, Kaiser CJO, Jagtap P, Kastenmüller A, Pischedda F, Marte A, von Zweydorf F, Vogt A, Giesert F, Pan L, Antonucci F, Kiel C, Zhang M, Weinkauf S, Sattler M, Sala C, Matteoli M, Ueffing M and Gloeckner CJ (2014). LRRK2 binds to neuronal vesicles through protein interactions mediated by its C-terminal WD40 domain. Mol. Cell. Biol. 34: 2147-2161.
  5. Muda K, Bertinetti D, Gesellchen F, Hermann JS, von Zweydorf F, Geerlof A, Jacob A, Ueffing M, Gloeckner CJ*, Herberg FW (2014). Parkinson-related LRRK2 mutation R1441C/G/H impairs PKA phosphorylation of LRRK2 and disrupts its interaction with 14-3-3. Proc. Natl Acad. Sci. U S A. 111:E34-43.
  6. Gillardon, F., Kremmer, E., Froehlich, T., Ueffing, M., Hengerer, B., Gloeckner, C.J. (2013) ATP-competitive LRRK2 inhibitors interfere with monoclonal antibody binding to the kinase domain of LRRK2 under native conditions. A method to directly monitor the active conformation of LRRK2? J. Neurosci. Methods. 214,62-68
  7. Piccoli, G., Condliffe, S.B., Bauer, M., Giesert, F., Boldt, K., De Astis, S., Meixner, A., Sarioglu, H., Vogt-Weisenhorn, D.M., Wurst, W., Gloeckner, C.J., Matteoli, M., Sala, C., Ueffing, M. (2011). LRRK2 controls synaptic vesicle storage and mobilization within the recycling pool. J Neurosci 31, 2225-2237.
  8. Meixner, A., Boldt, K., Van Troys, M., Askenazi, M., Gloeckner, C.J., Bauer, M., Marto, J.A., Ampe, C., Kinkl, N., and Ueffing, M. (2011). A QUICK screen for Lrrk2 interaction partners--leucine-rich repeat kinase 2 is involved in actin cytoskeleton dynamics. Mol Cell Proteomics 10, M110 001172.
  9. Gloeckner, C. J., Boldt, K., von Zweydorf, F., Helm, S., Wiesent, L., Sarioglu, H. and Ueffing, M. (2010). Phosphopeptide analysis reveals two discrete clusters of phosphorylation in the N-terminus and the Roc domain of the Parkinson-disease associated protein kinase LRRK2. J Proteome Res. 9, 1738-1745.
  10. Gloeckner, C. J., Schumacher, A., Boldt, K. and Ueffing, M. (2009). The Parkinson disease-associated protein kinase LRRK2 exhibits MAPKKK activity and phosphorylates MKK3/6 and MKK4/7, in vitro. J Neurochem. 109, 959-968.
  11. Gloeckner, C. J., Boldt, K., Schumacher, A., Roepman, R. and Ueffing, M. (2007). A novel tandem affinity purification strategy for the efficient isolation and characterisation of native protein complexes. Proteomics  7, 4228-4234.
  12. Gloeckner, C. J., Kinkl, N., Schumacher, A., Braun, R. J., O'Neill, E., Meitinger, T., Kolch, W., Prokisch, H. and Ueffing, M. (2006). The Parkinson disease causing LRRK2 mutation I2020T is associated with increased kinase activity. Hum Mol Genet. 15, 223-232.

 

For further publications of Dr. Johannes Gloeckner Lab see PubMed