Functional Kidney Proteomics

Our team uses proteomics tools to study renal physiology and pathophysiology. This method uses mass spectrometry data to study the entity of proteins within a cell, the proteome. We specifically analyze intracellular signaling networks in cells (interactome), and also discover molecular switches (phosphoproteome) and turnover mechanisms of important kidney proteins. Using quantitative proteomics, we discovered and characterized unanticipated signaling mechanisms in podocytes and cells of the distal nephron. We functionally validate proteomics-generated results and hypotheses using orthogonal biochemical, genetic and bioinformatics experiments.


We also apply methods to integrate multi-leveled omics datasets and transform the data into biologically meaningful paths of research. The ultimate goal of the highly translational group is to understand proteomic perturbations in renal cells on a systems level, thereby enabling targeted therapies in renal disease. We collaborate closely with the state-of-the-art proteomics core facility at the CECAD. Our group benefits from collaboration with several intramural, national and international groups.

Group leader

Dr. med. Markus Rinschen


  • Ruth Herzog
  • Priyanka Kohli

1. Rinschen, M.M., Pahmeyer, C., Pisitkun, T., Schnell, N., Wu, X., MaaSS, M., Bartram, M.P., Lamkemeyer, T., Schermer, B., Benzing, T., and Brinkkoetter, P.T. (2015). Comparative phosphoproteomic analysis of mammalian glomeruli reveals conserved podocin C-terminal phosphorylation as a determinant of slit diaphragm complex architecture. Proteomics. 15(7): p. 1326-31

2. Kohli, P., Bartram, M.P., Habbig, S., Pahmeyer, C., Lamkemeyer, T., Benzing, T., Schermer, B., and Rinschen, M.M. (2014). Label-free quantitative proteomic analysis of the YAP/TAZ interactome. Am J Physiol Cell Physiol. 306(9): p. C805-18.

3. Rinschen, M.M., Schermer, B., and Benzing, T. (2014). Vasopressin-2 Receptor Signaling and Autosomal Dominant Polycystic Kidney Disease: From Bench to Bedside and Back Again. Journal of the American Society of Nephrology. 25(6): p. 1140-1147

4. Rinschen, M.M., Wu, X., Konig, T., Pisitkun, T., Hagmann, H., Pahmeyer, C., Lamkemeyer, T., Kohli, P., Schnell, N., Schermer, B., Dryer, S., Brooks, B.R., Beltrao, P., Krueger, M., Brinkkoetter, P.T., and Benzing, T. (2014). Phosphoproteomic analysis reveals regulatory mechanisms at the kidney filtration barrier. J Am Soc Nephrol. 25(7): p. 1509-22.

5. Rinschen, M.M., Yu, M.J., Wang, G., Boja, E.S., Hoffert, J.D., Pisitkun, T., and Knepper, M.A. (2010). Quantitative phosphoproteomic analysis reveals vasopressin V2-receptor-dependent signaling pathways in renal collecting duct cells. Proc Natl Acad Sci U S A. 107(8): p. 3882-7.