The Bassermann Laboratory

    Department of Medicine III • Hematology/Oncology

Technische Universität München

Aberrant ubiquitin-dependent signaling in cancer

Our laboratory investigates principles of ubiquitin-dependent signaling in fundamental and cancer relevant cellular functions such as cell cycle control, DNA repair, transcription, protein synthesis, cell differentiation and apoptosis. In particular, we investigate how aberrations of these pathways contribute to tumor development and maintenance, having a focus on hematological malignancies such as multiple myeloma and lymphoma. Ultimately, our work aims to identify new therapeutic target structures to guide the development of rationally designed targeted therapies and biomarkers. To achieve these goals, we use an interdisciplinary approach that combines tumor genomics/functional proteomics and cell biology with translational analyses in preclinical mouse models and human tumor samples.

Selected Publications

Engel, K., Rudelius, M., Slawska, J., Ahangarian Abhari, B., Altmann, B., Kurutz, J., Brunner, A., Targosz, B.S., Loewecke, F., Knorn, A.M., Gloeckner, C.J., Ueffing, M., Fernandez-Sáiz, V., Fulda, S., Pfreundschuh, M., Trümper, L., Klapper, W., Keller, U., Jost, P.J., Rosenwald, A., Peschel, C., Bassermann, F. USP9X stabilizes XIAP to regulate mitotic cell death and mediate resistance to anti-tubulin chemotherapeutics in aggressive B-cell lymphoma. EMBO Mol. Med. (2016) in press

Eichner R., Heider M., Fernández-Sáiz V., v. Bebber F., Garz A.K., Lemeer S., Rudelius M., Targosz, B.S., Jacobs L., Knorn A.M., Slawska J., Platzbecker U., Germing U., Langer C., Knop S., Einsele H., Peschel C., Haass C., Keller U., Schmid B., Götze K.S., Kuster B., and Bassermann F. Immunomodulatory drugs disrupt the cereblon–CD147– MCT1 axis to exert antitumor activity and teratogenicity, Nature Medicine (2016). DOI: 10.1038/nm.4128

Baumann, U., Fernandez-Saiz, V., Rudelius, M., Lemeer, S., Rad, R., Knorn, A.M., Slawska, J., Engel, K., Jeremias, I., Li, Z., Tomiatti, V., Illert, A.L., Targosz, B.S., Braun, M., Perner, S., Leitges, M., Klapper, W., Dreyling, M., Miething, C., Lenz, G., Rosenwald, A., Peschel, C., Keller, U., Kuster, B., Bassermann, F. Disruption of the PRKCD-FBXO25-HAX-1 axis attenuates the apoptotic response and drives lymphomagenesis. Nature Medicine (2014) 20, 1401-1409.

Dechow, T., Steidle, S., Götze, K., Rudelius, M., Behnke, K., Pechloff, K., Kratzat, S., Bullinger, L., Fend, F., Soberon, V., Mitova, N., Li, Z., Thaler, M., Bauer, J., Pietschmann, E., Albers, C., Grundler, R., Schmidt-Supprian, M., Ruland, J., Peschel, C., Duyster, J., Rose-John, S., Bassermann, F., and Keller, U. gp130 activation induces myeloma and collaborates with Myc. J. Clin. Invest, (2014), 124, 5263-5274.

Bassermann, F., Eichner, R., Pagano, M. The ubiquitin proteasome system – Implications for cell cycle control and the targeted treatment of cancer. BBA-Mol Cell Res (2014) 184, 150-62

Fernández-Sáiz, V., Targosz, B.S., Lemeer, S., Eichner, R, Langer, C., Bullinger, L., Reiter, C., SlottaHuspenina, J., Schroeder, S., Knorn, A.M., Kurutz, J., Peschel, C., Pagano, M., Kuster, B., and Bassermann, F. SCFFbxo9 and CK2 direct the cellular response to growth factor withdrawal via Tel2/Tti1 degradation and promote survival in multiple myeloma. Nature Cell. Biol. (2013) 15, 72–81.

Dehan, E., Bassermann, F., Guardavaccaro, D., Vasiliver-Shamis, G., Cohen, M., Lowes, K., Dustin, M., Huang, D., Taunton, J., and Pagano, M. βTrCP- and Rsk1/2-mediated degradation of BimEL inhibits apoptosis.
 Mol Cell (2009) 33, 109-116.

Bassermann, F., Frescas, D., Guardavaccaro, D., Busino, L., Peschiaroli, A., Pagano, M. The Cdc14B-Cdh1-Plk1 axis controls the G2 DNA damage response checkpoint. Cell (2008) 134, 256-267.

Frescas, D., Guardavaccaro, D., Bassermann, F., Koyama-Nasu, R., Pagano, M. The histone demethylase JHDM1B is a nucleolar protein that represses transcription of ribosomal RNA genes. Nature (2007) 450, 309-313.

Busino, L., Bassermann, F., Maiolica, A., Lee, C., Nolan, P. M., Godinho, S. I., Draetta, G. F., and Pagano, M. SCF-Fbxl3 controls the oscillation of the circadian clock by directing the degradation of cryptochrome proteins. Science (2007) 316, 900-904.

Bassermann, F., von Klitzing, C., Illert, A. L., Munch, S., Morris, S. W., Pagano, M., Peschel, C., and Duyster, J. Multisite phosphorylation of nuclear interaction partner of ALK (NIPA) at G2/M involves cyclin B1/Cdk1. J. Biol. Chem. (2007) 282, 15965-15972.

Bassermann, F., von Klitzing, C., Muench, S., Bai, R.Y., Kawaguchi, H., Morris, S.W., Peschel, C., and Duyster, J. NIPA defines an SCF-type mammalian E3 ligase that regulates mitotic entry. Cell (2005) 122, 45-57.