B07 - Structural and functional study of mixed lineage kinase domain-like proteins in plants and animals
Jijie Chai
Institute for Biochemistry, University of Cologne
Contact: jchai
uni-koeln.de
For more information visit: Chai lab
Takaki Maekawa
The Institute for Plant Sciences, University of Cologne
Contact: takaki.maekawauni-koeln.de
For more information visit: Maekawa lab
Ana J. Garcia-Saez
Institute for genetics, CECAD, University of Cologne
Contact: garcia-officeuni-koeln.de
For more information see: Garcia-Saez lab
Abstract
The discovery of a new protein family in seed plants that is structurally and functionally homologous to animal Mixed lineage kinase domain-like (MLKL) protein, the executioner of necroptosis in animal cells, provided evidence that similar mechanisms may induce plasma membrane permeabilisation in plants and animals. This project aims to understand the molecular principles of MLKL-mediated cell death and immunity by determining and comparing the nanoscale organisation and cellular dynamics of this protein family in plant and animal cells.
Project related Publications
Wang, J., Hu, M., Wang, J., Qi, J., Han, Z., Wang, G., Qi, Y., Wang, H.W., Zhou., J.M., and Chai, J. (2019). Reconstitution and structure of a plant NLR resistosome conferring immunity. Science. 364, pii: eaav5870.
Danial, J.S.H., and Garcia-Saez, A.J. (2019) Quantitative analysis of super-resolved structures using ASAP. Nat Methods (accepted)
Jacob, F., Kracher, B., Mine, A., Seyfferth C., Blanvillain-Baufumé., S., Parker, J.E., Tsuda, K., Schulze-Lefert, P.*, and Maekawa, T.* (2018). A dominant-interfering camta3 mutation compromises primary transcriptional outputs mediated by both cell surface and intracellular immune receptors in Arabidopsis thaliana. New Phytol. 217, 1667-1680. *Co-corresponding authors.
Ros, U., Peña-Blanco, A., Hänggi, K., Kunzendorf, U., Krautwald, S., Wong, W.W.-L., and Garcia-Saez, A.J. (2017). Necroptosis execution is mediated by plasma membrane nanopores independent of calcium. Cell Rep. 19, 175-187.
Salvador-Gallego, R., Mund, M., Cosentino, K., Schneider, J., Unsay, J., Schraermeyer, U., Engelhardt, J., Ries, J.*, and Garcia-Saez, A.J.* (2016). Bax assembly into rings and arcs in apoptotic mitochondria is linked to membrane pores. EMBO J. 35, 389-401. * Co-corresponding author.
Hu, Z., Zhou, Q., Zhang, C., Fan, S., Cheng, W., Zhao, Y., Shao, F., Wang, H.W., Sui, S.F., and Chai, J. (2015). Structural and Biochemical Basis for Induced Self-propagation of a NOD-like Receptor. Science 350, 399-404.
Subburaj, Y., Cosentino, K., Axmann, M., Pedrueza-Villalmanzo, E., Hermann, E., Bleicken, S., Spatz, J., and Garcia-Saez, A.J. (2015). Bax monomers form dimer units in the membrane that further self-assemble into multiple oligomeric species. Nat. Commun. 6, 8042.
Hao W, Collier SM, Moffett P, and Chai J. (2013) Structural basis for the interaction between the potato virus X resistance protein (Rx) and its cofactor Ran GTPase-activating protein 2 (RanGAP2). J Biol Chem. 13, 35868-35876.
Maekawa, T., Cheng, W., Spiridon, L.N., Töller, A., Lukasik, E., Saijo, Y., Liu, P., Shen, Q.H., Micluta, M.A., Somssich, I.E., Takken, F.L., Petrescu, A.J., Chai, J*., and Schulze-Lefert, P*. (2011). Coiled-coil domain-dependent homodimerization of intracellular barley immune receptors defines a minimal functional module for triggering cell death. Cell Host Microbe 9, 187-199. * Co-corresponding author.
Mahdi,L.K., Huang, M., Zhang, X., Nakano R.-T., Kopp, L.B., Saur, I. M.-L., Jacob, F., Kovacova, V., Lapin, D., , Murphy, J., Parker, J., Hofmann, K., Schulze-Lefert. P, Chai. J., and T. Maekawa (2019). Plant mixed lineage kinase domain-like proteins limit biotrophic pathogen growth, BioRxiv doi: https://doi.org/10.1101/681015