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

The structure of a pannexin 1 uncovers the extracellular loops of pannexin 1 as important structural motifs for ion selectivity and channel inhibition.

Purified Pannexin 1 channels activated by caspase cleavage in proteoliposomes reconstitute a permeation pathway for intercellular signaling molecules important in inflammation and cell clearance.

Autocrine activation of macrophages is modulated by Connexin-43-mediated ATP release in response to TLR-4 and -2 agonists in a P2Y1-dependent manner, ultimately determining sepsis survival.

N-glycans commonly present in the protease domains are required for calnexin-mediated protein folding and intracellular trafficking.

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

Cleavage of pannexin-1 channel by caspases facilitates the loss of intracellular ATP level and attenuates glycolytic metabolism of apoptotic cells.

The structure of pannexin 1, a channel protein with a large pore, has been determined for the first time.

Melanophores and xanthophores interact via heteromeric gap junctions composed of Connexin 41.8 and Connexin 39.4 to establish the adult pigment pattern in zebrafish.

A novel role of endosomal machineries retromer and ESCRT in membrane delivery of Drosophila septate junction components is required for maintenance of junction integrity and epithelial barrier function.