Connexin 43 hemichannel activation associated with prostaglandin release in osteocytes plays an important role in anabolic function of mechanical loading on bone tissue and hemichannels could be a potential new therapeutic target for treating bone loss and osteoporosis.

Building on previous work (Meigh et al., 2013) we show that A88V, a mutation in connexin26 (Cx26) that causes Keratitis-Ichthyosis-Deafness (KID) syndrome in humans, is linked to a lack of sensitivity to CO₂ by Cx26 hemichannels.

The innexin protein UNC-7, a homologue of vertebrate pannexins, plays a specific, gap junction-independent role in C. elegans mechanosensation.

A CO₂ receptor and a mechanism for the CO₂-mediated opening of gap junction hemichannels have been identified.

The mutation of Lys125 in connexin26 to glutamate, a carbamylation mimetic, pushes the equilibrium of the gap junction channel seen in cryo-EM towards a more closed conformation.

Cryo-EM structures and molecular dynamics simulations of Cx43 gap junction channel and hemichannel reveal a putative closed state.

Mitochondrial Cx43 hemichannels regulate ATP generation by mediating K+, H+, and ATP transfer across the mitochondrial inner membrane and the interaction with mitochondrial ATP synthase, contributing to maintenance of mitochondrial redox and cell protection under oxidative stress.

An in silico analysis of gap junction proteins supports the hypothesis that connexins replaced the primordial innexins in chordate gap junctions due to an evolutionary bottleneck.

Ano1 deletion disrupts Ca²⁺ waves within Kölliker’s organ, reduces burst-firing activity and frequency selectivity of auditory brainstem neurons in the medial nucleus of the trapezoid body, and impairs the functional refinement of its projections to the lateral superior olive.

Anatomical study reveals a new perspective on the definition of an electrical synapse where, in addition to the communicating role of gap junctions, additional cellular structures might be involved in the support and regulation of these intercellular channels.