Universität zu Köln 

Central BioAnalytics
Zentrum für Molekulare Medizin Köln, Universitätsklinikum Köln
website

Proteomics Facility
CECAD Research Center/Institut für Genetik, Universität zu Köln
within the SFB 635 since July 2011
website

Research groups of the SFB 635 are supported by two mass spectrometry units, the Central BioAnalytics (CBA, F.G. Hanisch) of the interfaculty Zentrum für Molekulare Medizin Köln (ZMMK) and, since 2008, the Proteomics Mass Spectrometry Facility of the excellence cluster CECAD (T. Lamkemeyer, until 12/2014). Both facilities provide a range of mass spectrometric applications, including protein identifications by LC-MS. In accordance with the topic of the SFB 635 one major focus of both facilities is the site-specific analysis of posttranslational modifications and terminal protein sequencing. Moreover, for several projects the amount of proteins in different samples has to be quantified on a relative basis, e.g. to reveal novel protein interaction partners. In this context, the CBA offers quantifications based on chemical peptide labelling (iTRAQ), whereas the complementary instrumentation and expertise of the CECAD group is specialising in in vivo strategies based on metabolic stable isotope labelling (SILAC).

Of the 18 SFB 635 research groups mass spectrometric technologies for analyses of posttranslational modifications and quantifications will be crucial for the success of at least 16 projects. Based on the experience of the last years these projects often necessitate the establishment of specialised methods in addition to already available high throughput techniques. Therefore, both facilities will expand the set of available methods, in particular for PTM analyses and quantifications, and increase the analytical capacity to cope with the increased demands. To meet these requirements the units are equipped with state-of-the-art ESI and MALDI instruments for the performance of all gel-based and LC-based mass spectrometric proteomic applications.

Running time: 2003 – 2015

Recent publications:

Seeger-Nukpezah T., Liebau M.C., Höpker K., Lamkemeyer T., Benzing T., Golemis E.A., Schermer B. (2012). The centrosomal kinase plk1 localizes to the transition zone of primary cilia and induces phosphorylation of nephrocystin-1. PLoS One. ;7(6):e38838. Epub 2012 Jun 11.

Steinfeldt, T., Könen-Waismann, S., Tong, L., Pawlowski, N., Lamkemeyer, T., Sibley, L.D., Hunn, J., and Howard, J. (2010). Phosphorylation of mouse immunity-regulated GTPase (IRG) resistance proteins is an evasion strategy for virulent Toxoplasma gondii. PLoS Biol. 8 (12), e1000576.

Jackson, L.P., Kelly, B.T., McCoy, A.J., Gaffry, T., James, L.C., Collins, B.M., Höning, S., Evans, P.R., and Owen, D.J. (2010). A large-scale conformational change couples membrane recruitment to cargo binding in the AP2 clathrin adaptor complex. Cell 141, 1220-1229.

Albert, T.K., Laubinger, W., Müller, S., Hanisch, F.-G., Kalinski, T., Meyer, F., Hoffmann, and W. (2010). Human intestinal TFF3 forms disulfide-linked heteromers with the mucus-associated FCGBP protein and is released by hydrogen sulfide. J. Proteome Res. 9, 3108-3117.

Lambeck, I., Chi, J.C., Krizowski, S., Mueller, S., Mehlmer, N., Teige, M., Fischer, K., and Schwarz, G. (2010). Kinetic analysis of 14-3-3-inhibited Arabidopsis thaliana nitrate reductase. Biochemistry 49, 8177-8186.

Roth, U., Razawi, H., Hommer, J., Engelmann, K., Schwientek, T., Müller, S., Baldus, S.E., Patsos, G., Corfield, A.P., Paraskeva, C., and Hanisch, F.-G. (2010). Differential expression proteomics of colorectal cancer based on a syngeneic cellular model for the progression of adenoma to carcinoma. Proteomics 10, 194-202.

Bulankina, A.V., Deggerich, A., Wenzel, D., Mutenda, K., Wittmann, J.G., Rudolph, M.G., Burger, K.N., and Höning, S. (2009). TIP47 functions in the biogenesis of lipid droplets. J. Cell Biol. 185, 641-655.

Chung, B.D., Kayserili, H., Ai, M., Freudenberg, J., Üzümcü, A., Uyguner, O., Bartels, C.F., Höning, S., Ramirez, A., Hanisch, F.-G., et al. (2008). A mutation in the signal sequence of LRP5 in a family with an osteoporosis-pseudoglioma syndrome (OPPG)-like phenotype indicates a novel disease mechanism for trinucleotide repeats. Hum. Mutation 30, 641-648.

Breloy, I., Schwientek, T., Gries, B., Razawi, H., Macht, M., Albers, C., and Hanisch, F.-G. (2008). Initiation of mammalian O-mannosylation in vivo is independent of a consensus sequence and controlled by peptide regions within and upstream of the alpha-dystroglycan mucin domain. J. Biol. Chem. 283, 18832-18840.