Structure versus function: Are new conformations of pannexin 1 yet to be resolved?

Carsten Mim, Guy Perkins, Gerhard Dahl

Research output: Contribution to journalArticlepeer-review

8 Scopus citations


Pannexin 1 (Panx1) plays a decisive role in multiple physiological and pathological settings, including oxygen delivery to tissues, mucociliary clearance in airways, sepsis, neuropathic pain, and epilepsy. It is widely accepted that Panx1 exerts its role in the context of purinergic signaling by providing a transmembrane pathway for ATP. However, under certain conditions, Panx1 can also act as a highly selective membrane channel for chloride ions without ATP permeability. A recent flurry of publications has provided structural information about the Panx1 channel. However, while these structures are consistent with a chloride selective channel, none show a conformation with strong support for the ATP release function of Panx1. In this Viewpoint, we critically assess the existing evidence for the function and structure of the Panx1 channel and conclude that the structure corresponding to the ATP permeation pathway is yet to be determined. We also list a set of additional topics needing attention and propose ways to attain the large-pore, ATP-permeable conformation of the Panx1 channel.

Original languageEnglish (US)
Article numbere202012754
JournalJournal of General Physiology
Issue number5
StatePublished - May 3 2021
Externally publishedYes

ASJC Scopus subject areas

  • Physiology


Dive into the research topics of 'Structure versus function: Are new conformations of pannexin 1 yet to be resolved?'. Together they form a unique fingerprint.

Cite this