These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Investigation via ion pore transplantation of the putative relationship between glutamate receptors and K+ channels.
    Author: Hoffmann J, Villmann C, Werner M, Hollmann M.
    Journal: Mol Cell Neurosci; 2006 Dec; 33(4):358-70. PubMed ID: 17011207.
    Abstract:
    The pore domains of ionotropic glutamate receptors (iGluRs) and potassium channels (K(+) channels) show several structural similarities. To test for functional compatibility, we transferred pore regions from prokaryotic, invertebrate, and vertebrate K(+) channels into pharmacologically representative iGluRs and vice versa. Although the chimeric proteins were expressed on the cell surface, only one of 45 pore chimeras showed ion channel function: The kainate receptor subunit GluR6, carrying the pore loop plus adjacent transmembrane domains of the prokaryotic, glutamate-gated, K(+)-selective GluR0, adopted several electrophysiological properties of the donor pore upon pore transplantation. This suggests that, despite structural similarities between iGluR and K(+) channel pores, there is a lack of functional compatibility so that K(+) channel pores cannot be gated by the iGluR gating machinery, and vice versa. However, K(+)-selective pores can be gated in an iGluR sequence environment, given a similar signal transduction mechanism as appears to be present in GluR0.
    [Abstract] [Full Text] [Related] [New Search]