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

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

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.

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

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.

The presence of cenexin at the old centrosome imposes a functional asymmetry on the mitotic spindle that impacts chromosome alignment and segregation.

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

Calcium release from the endoplasmic reticulum through the IP₃ receptor ion channel is strongly regulated by a calcium-binding protein in the lumen of the endoplasmic reticulum.