Supplementary Materials

Supplementary Materials for:

A Plant Homolog of Animal Glutamate Receptors Is an Ion Channel Gated by Multiple Hydrophobic Amino Acids

Daniel Tapken,* Uta Anschütz, Lai-Hua Liu, Thomas Huelsken, Guiscard Seebohm, Dirk Becker, Michael Hollmann*

*Corresponding author. E-mail: daniel.tapken{at}rub.de (D.T.); michael.hollmann@rub.de (M.H.)

This PDF file includes:

  • Fig. S1. pH dependence of methionine-induced AtGLR1.4-mediated currents.
  • Fig. S2. Representative current responses of AtGLR1.4 upon application of signaling molecules that occur in plants.
  • Fig. S3. Sequence alignment of the LBDs of AtGLR1.4 and GluN1.
  • Fig. S4. Sequence alignment of the most conserved region of the LBDs of Arabidopsis iGluR homologs and rat iGluRs.
  • Fig. S5. Localization of AtGLR1.4 in HEK293 cells.
  • Fig. S6. Localization of AtGLR1.4 in mesophyll protoplasts isolated from Arabidopsis leaves.
  • Fig. S7. Phylogenetic tree of the LBDs of iGluRs and related proteins.
  • Table S1. GenBank accession numbers of iGluRs and related proteins used for phylogenetic analysis.
  • Reference (58)

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Citation: D. Tapken, U. Anschütz, L.-H. Liu, T. Huelsken, G. Seebohm, D. Becker, M. Hollmann, A Plant Homolog of Animal Glutamate Receptors Is an Ion Channel Gated by Multiple Hydrophobic Amino Acids. Sci. Signal. 6, ra47 (2013).

© 2013 American Association for the Advancement of Science