Subunit requirements for Torpedo AChR channel expression

A specific role for the δ-subunit in voltage-dependent gating

M. D. Golino, Owen Hamill

Research output: Contribution to journalArticle

6 Citations (Scopus)

Abstract

This study examines the subunit requirement for Torpedo acetylcholine receptor (AChR) channel expression and the influence of non-α-subunit deletions on single AChR-channel currents. Xenopus oocytes injected with subunit combinations deficient in single non-α-subunit mRNA transcripts display the following order of ACh sensitivity: β-less > γ-less > δ-less. Oocytes injected with only the α-subunit and one non-α-subunit display the order: αδ > αγ > αβ. These sequences indicate the effectiveness of non-α-subunit substitution is δ > γ > β. Single AChR-channel currents measured in oocytes deficient in either β or γ display conductance and voltage-sensitive burst kinetics similar to the wild-type channel. In contrast, the δ-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 δ-subunit or its specific interactions with the α-subunit contribute to the voltage-dependent gating of the Torpedo AChR channel.

Original languageEnglish (US)
Pages (from-to)297-309
Number of pages13
JournalThe Journal of Membrane Biology
Volume129
Issue number3
DOIs
StatePublished - Sep 1992
Externally publishedYes

Fingerprint

Torpedo
Cholinergic Receptors
Oocytes
Xenopus
Messenger RNA

Keywords

  • expression
  • single-channel currents
  • subunit function
  • Torpedo AChR
  • Xenopus oocyte

ASJC Scopus subject areas

  • Physiology
  • Cell Biology
  • Biophysics

Cite this

Subunit requirements for Torpedo AChR channel expression : A specific role for the δ-subunit in voltage-dependent gating. / Golino, M. D.; Hamill, Owen.

In: The Journal of Membrane Biology, Vol. 129, No. 3, 09.1992, p. 297-309.

Research output: Contribution to journalArticle

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N2 - This study examines the subunit requirement for Torpedo acetylcholine receptor (AChR) channel expression and the influence of non-α-subunit deletions on single AChR-channel currents. Xenopus oocytes injected with subunit combinations deficient in single non-α-subunit mRNA transcripts display the following order of ACh sensitivity: β-less > γ-less > δ-less. Oocytes injected with only the α-subunit and one non-α-subunit display the order: αδ > αγ > αβ. These sequences indicate the effectiveness of non-α-subunit substitution is δ > γ > β. Single AChR-channel currents measured in oocytes deficient in either β or γ display conductance and voltage-sensitive burst kinetics similar to the wild-type channel. In contrast, the δ-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 δ-subunit or its specific interactions with the α-subunit contribute to the voltage-dependent gating of the Torpedo AChR channel.

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