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

Search MEDLINE/PubMed


  • Title: Subunit requirements for Torpedo AChR channel expression: a specific role for the delta-subunit in voltage-dependent gating.
    Author: Golino MD, Hamill OP.
    Journal: J Membr Biol; 1992 Sep; 129(3):297-309. PubMed ID: 1433281.
    Abstract:
    This study examines the subunit requirement for Torpedo acetylcholine receptor (AChR) channel expression and the influence of non-alpha-subunit deletions on single AChR-channel currents. Xenopus oocytes injected with subunit combinations deficient in single non-alpha-subunit mRNA transcripts display the following order of ACh sensitivity: beta-less > gamma-less > delta-less. Oocytes injected with only the alpha-subunit and one non-alpha-subunit display the order: alpha delta > alpha gamma > alpha beta. These sequences indicate the effectiveness of non-alpha-subunit substitution is delta > gamma > beta. Single AChR-channel currents measured in oocytes deficient in either beta or gamma display conductance and voltage-sensitive burst kinetics similar to the wild-type channel. In contrast, the delta-less combination express channels with burst kinetics that are relatively faster and voltage insensitive. These results indicate that either a specific structural domain in the delta-subunit or its specific interactions with the alpha-subunit contribute to the voltage-dependent gating of the Torpedo AChR channel.
    [Abstract] [Full Text] [Related] [New Search]