Professor Veit Flockerzi

My laboratory focuses on the molecular processes underlying receptor-ion channel-coupling, particularly in heart and smooth muscle cells. Current studies seek to understand the role of specific transient receptor potential (TRP) channels in cellular excitation as well as the functions of β-subunits (CaVβ) of voltage-gated calcium channels which are independent of CaVα1, the ion conducting pore of these channels. Techniques used to study these processes include gene targeting, identification of novel genes through genomics screens, patch clamp measurements of ion channel function, Ca imaging, and protein biochemistry.

A major goal of the laboratory is to identify genes encoding channel proteins and relating signalling molecules involved in muscle biology and to determine their functions in health and disease. An additional effort in the laboratory is to combine genetics, protein chemistry and pharmacological procedures to advance the understanding of physiological processes.

Selected publications

• Flockerzi, V., Oeken, H.-J., Hofmann, F., Pelzer, D., Cavalié, A. and Trautwein, W. (1986)
  Purified dihydropyridine-binding site from skeletal muscle t-tubules is a functional calcium channel.
  Nature 323, 66-68
• Tanabe, T., Takeshima, H., Mikami, A., Flockerzi, V., Takahashi, H., Kangawa, K., Kojima, M., Matsuo, H., Hirose, T. and Numa, S. (1987)
  Primary structure of the receptor for calcium channel blockers from rabbit skeletal muscle.
  Nature 328, 313-318
• Ruth, P., Röhrkasten, A., Biel, M., Bosse, E., Regulla, S., Meyer, H.E., Flockerzi, V. and Hofmann, F. (1989)
  Primary structure of the β-subunit of the DHP-sensitive calcium channel from skeletal muscle.
  Science 245, 1115-1118
• Philipp, S., Cavalié, A., Freichel, M., Wissenbach, U., Zimmer, S., Trost, C., Marquart, A., Murakami, M. and Flockerzi, V. (1996)
  A mammalian capacitative calcium entry channel homologous to Drosophila TRP and TRPL.
  EMBO J. 15, 6166-6171
• Montell, C., Birnbaumer, L. and Flockerzi, V. (2002)
  The TRP channels, a remarkable functional family.
  Cell 108, 595-598
• Berggren, P.-O., Yang, S.-N., Murakami, M., Efanov, A.M., Uhles, S., Köhler, M., Moede, T., Fernström, A., Appelskog, I.B., Aspinwall, C.A., Zaitsev, S.V., Larsson, O., Moitoso de Vargas, L., Fecher-Trost, C., Weißgerber, P., Ludwig, A., Leibiger, B., Juntti-Berggren, L., Barker, C.J., Gromada, J., Freichel, M., Leibiger, I.B. and Flockerzi, V. (2004)
  Removal of Ca²⁺ channel β3 subunit enhances Ca2+-oscillation frequency and insulin exocytosis.
  Cell 119, 273-284
• Vennekens, R., Olausson, J., Meissner, M., Bloch, W., Mathar, I., Philipp, S.E., Schmitz, F., Weissgerber, P., Nilius, B., Flockerzi, V., Freichel, M. (2007)
  Increased IgE-dependent mast cell activation and anaphylactic reponses in mice lacking the calcium-activated nonselective cation channel TRPM4.
  Nature Immunology 8, 312-320
• Gerzanich, V., Woo, S.K., Vennekens, R., Tsymbalyuk, S.O., Ivanova, S., Ivanov, A., Geng, Z., Chen, Z., Nilius, B., Flockerzi, V., Freichel, M., Simard, J.M. (2009)
  De novo expression of TRPM4 initiates secondary hemorrhage in spinal cord injury.
  Nature Medicine (in print)