The Amino Terminal Domain and Modulation of Connexin36 Gap Junction Channels by Intracellular Magnesium Ions.

ABSTRACT: Electrical synapses between neurons in the mammalian CNS are predominantly formed of the connexin36 (Cx36) gap junction (GJ) channel protein. Unique among GJs formed of a number of other members of the Cx gene family, Cx36 GJs possess a high sensitivity to intracellular Mg²⁺ that can robustly act to modulate the strength of electrical synaptic transmission. Although a putative Mg²⁺ binding site was previously identified to reside in the aqueous pore in the first extracellular (E1) loop domain, the involvement of the N-terminal (NT) domain in the atypical response of Cx36 GJs to pH was shown to depend on intracellular levels of Mg²⁺. In this study, we examined the impact of amino acid substitutions in the NT domain on Mg²⁺ modulation of Cx36 GJs,

SUBMITTER: Kraujalis T 

PROVIDER: S-EPMC8899287 | biostudies-literature | 2022

REPOSITORIES: biostudies-literature