Dr. rer. nat. Robert Lindner
Education and Professional Experience
- 1982–1988 Studied biology at the Technical University and Ludwig Maximilian University, Munich
- 1987–1992 Master’s thesis and doctoral dissertation in the research group of Dr. Ernst Ungewickell, Max Planck Institute for Biochemistry, Martinsried
- 1992–1997 Postdoctoral fellow in the research group of Dr. Emil Unanue, Washington University School of Medicine, St. Louis, MO (USA)
- 1997–2000 Research group leader (C1), Institute of Genetics, University of Bonn
- Since 2000: Group Leader , Institute of Cell Biology, merged in 2016 to form the Institute of Neuroanatomy and Cell Biology
Awards
- 1982–1987 Scholarship from the Bavarian Program for the Promotion of Gifted Students
- 1985–1987 Scholarship from the German National Academic Foundation
- 1992–1994 DFG International Fellowship
- 2024 Teaching Award from the Student Body, 2nd Year of dentistry
Memberships:
- Since 1993: American Society for Cell Biology (ASCB)
- Since 2005 German Society for Cell Biology (DGZ)
Teaching
- Human medicine study programme: Cell Biology and Microscopic Anatomy (2000–2024)
- Study programme in dentistry: Microscopic Anatomy (since 2022)
- Master’s programs in Biomedicine (2012–2024) and Biochemistry (since 2012): Cell Biology and Electron Microscopy
- Bachelor’s program in Biology: Immunology (2000–2011)
- PhD Program in "Molecular Medicine": Cell Biology/Membrane Domains (2000–2025)
Additional Qualifications and Activities
- 2001 Genetic Engineering Safety Course , Project Leader S1
- 2009 Training on the FEI Tecnai electron microscope/Eindhoven
- 2009–2013 Technical Director of the Central EM Laboratory (with Dr. S. Groos)
- 2011–2012 University Teaching Program "Active in Teaching"
- 2012–2015 Adjunct Lecturer for the module “Fundamentals of Cell Biology in Medicine”
- 2014–2024 Module coordinator for cell biology in the master’s programs in biomedicine and biochemistry
- Since 2014 Radiation Safety AuthorisedRepresentative
- Since 2015: Authorised Representative for Occupational Safety
- 2020 Expertise in Animal Experimentation Methods
Research Focus
- Intracellular transport processes
Following my Ph.D. and several studies on coat proteins of clathrin-coated membrane vesicles, this field became my primary research focus.
- Antigen Presentation and Membrane Domains
As a PostDoc in Dr. Emil Unanu’s laboratory in St. Louis, I worked on several projects regarding intracellular loading pathways of MHC II molecules, including the development of a method to track antigen processing and the loading of MHC II molecules in cells. Using this technique, it was possible for the first time to detect two distinct MHC II loading pathways in B lymphocytes based on their loading products. Subsequent work by my own research group in Bonn and Hanover focused on the access of MHC molecules to MHC loading compartments and the functions of membrane domains in the transport of MHC molecules. Another project focused on the cytokine MIF, which induces the fusion of membrane domains composed of newly synthesized MHC II and antigen-binding B-cell receptors, thereby triggering co-endocytosis.
- Pathomechanisms of neurodegenerative diseases
Following the merger of the Institute of Cell Biology with the Institute of Neuroanatomy, the focus shifted to the question of whether changes in endocytosis occur in spinal muscular atrophy (SMA). SMA is a severe neurodegenerative disease that leads to the death of motor neurons and the degeneration of skeletal muscle. We have identified a novel macropinocytosis pathway in motor neurons that is upregulated in SMA and were able to decipher the pathomechanism underlying this regulation. Macropinocytosis leads to the degradation of receptors of a retrograde signaling pathway from skeletal muscle cells to presynaptic nerve terminals of motor neurons. Since retrograde signals provide essential feedback for the maintenance of neuromuscular synapses and motor neurons, our finding explains why SMA originates in these cells. How exactly the newly discovered macropinocytosis pathway functions, whether other receptors are affected by it, and whether this mechanism also plays a role in other neurodegenerative diseases will be the subject of future investigations.
Selected References
Rademacher, S., Detering, N.T., Schüning, T., Lindner, R., Santonicola, P., Wefel, I.M., Dehus, J., Walter, L.M., Brinkmann, H., Niewienda, A., Janek, K., Varela, M.A., Bowerman, M., Di Schiavi, E., Claus, P. (2020). A single amino acid residue regulates PTEN-binding and stability of the spinal muscular atrophy protein SMN. Cells, doi:10.3390/cells9112405.
Schöttelndreier, D., Langejürgen, A., Lindner, R., & Genth, H. (2020). Low density lipoprotein receptor-related protein-1 (LRP1) is involved in the uptake of Clostridioides difficile toxin A and serves as an internalizing receptor. Front. Cell. Infect. Microbiol. 10, 565465.
Walter, L.M., Franz, P., Lindner, R., Tsiavaliaris, G., Hensel, N., Claus, P. (2019) Profilin2a phosphorylation as a regulatory mechanism for actin dynamics. FASEB J. 34, 2147–2160.
Schöttelndreier, D., Seeger, K., Grassl, G.A., Winny, M.R., Lindner, R., and Genth, H. (2018) Expression and (lack of) internalization of cell surface receptors of Clostridioides difficile Toxin B. Front. Microbiol. 9, 1483.
Lindner, R. (2017). Invariant chain complexes and clusters as platforms for MIF signaling. Cells 6, 6.
Sörensen-Zender, I., Bhayana, S., Susnik, N., Rolli, V., Batkai, S., Baisantry, A., Bahram, S., Sen, P., Teng, B., Lindner, R., Schiffer, M., Thum, T., Melk, A., Haller, H., and Schmitt, R. (2015) J. Am. Soc. Nephrol. 26, 2659–2668.
Hauser, J.T. and Lindner, R. (2014) Coalescence of B cell receptor and invariant chain-MHC II in a raft-like membrane domain. J. Leukocyte Biol. 96, 843-855.
Chaturvedi, A., Araujo Cruz, M.M., Jyotsana, N., Sharma, A., Yun, H., Görlich, K., Wichmann, M., Schwarzer, A., Preller, M., Thol, F., Meyer, J., Haemmerle, R., Struys, E.A., Jansen, E.E., Modlich, U., Li, Z., Sly, L.M., Geffers, R., Lindner, R., Manstein, D.J., Lehmann, U., Krauter, J., Ganser, A., Heuser, M. (2013) Mutant IDH1 promotes leukemogenesis in vivo and can be specifically targeted in human AML. Blood, 122, 2877-2887.
Lindner, R. and Naim, H.Y. (2009). Domains in biological membranes. Exp. Cell Res. 315, 2871-2878.
Lindner, R. and Knorr, R. (2009). Rafting trips into the cell. Commun. Integr. Biol. 2, 420-421.
Knorr, R., Karacsonyi, C., and Lindner, R. (2009). Endocytosis of MHC molecules by distinct membrane rafts. J. Cell Sci. 122, 1584–1594.
Karacsonyi, C., Bedke, T., Hinrichsen, N., Schwinzer, R., and Lindner, R. (2005). MHC II molecules and invariant chain reside in membranes distinct from conventional lipid rafts. J. Leukocyte Biol. 78, 1097–1105.
Karacsonyi, C., Knorr, R., Fülbier, A., and Lindner, R. (2004). Association of MHC II with cholesterol- and sphingolipid-rich membranes precedes peptide loading. J. Biol. Chem. 279, 34818–34826.
Lindner, R. (2002). Transient surface delivery of invariant chain-MHC II complexes via endosomes: a quantitative study. Traffic 3, 133-146.
Lindner, R. (2001). One-step separation of endocytic organelles,Golgi/trans-Golgi network, and plasma membrane by density gradient electrophoresis. Electrophoresis 22, 386–393.
Parra-Lopez, C.A., Lindner, R., Vidavsky, I., Gross, M., and Unanue, E.R. (1997). Presentation on class II MHC molecules of endogenous lysozyme targeted to the endocytic pathway. J. Immunol. 158, 2670–2679.
Lindner, R. and Unanue, E.R. (1996). Distinct antigen-MHC class II-complexes generated by separate processing pathways. EMBO J. 15, 6910-6920.
Ungewickell, E., Ungewickell, H., Holstein, S.E.H., Lindner, R., Prasad, K., Barouch, W., Martin, B., Greene, L.E., and Eisenberg, E. (1995). Role of auxilin in uncoating clathrin-coated vesicles. Nature 378, 632–635.
Lindner, R. and Ungewickell, E. (1992). Clathrin-assembly proteins of bovine brain coated vesicles: An evaluation of their number and assembly-promoting activity. J. Biol. Chem. 267, 16567–16573.
Lindner, R. and Ungewickell, E. (1991). Light chain-independent binding of adaptors, AP180 and auxilin to clathrin. Biochemistry 30, 9097-9101.
Online Profile:
ORCID: 0000-0002-6421-5778