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ATP and large signaling metabolites flux through caspase-activated Pannexin 1 channels

by Gaete, Pablo S , Contreras, Jorge E , Oleniacz, Patrycja W , Medina, Christopher B , Jin, Xueyao , Narahari, Adishesh K , Barrett, Paula Q , Kiessling, Volker , Bayliss, Douglas A , Leonhardt, Susan A , Yeager, Mark , Tamm, Lukas K , Ravichandran, Kodi S , Kreutzberger, Alex JB , Chiu, Yu-Hsin

in Adenosine Triphosphate - metabolism / Animals / Apoptosis / Caspase / Caspases - metabolism / Chromatography / Connexins - genetics / Connexins - metabolism / Humans / ion channels / Ion Channels - genetics / Ion Channels - metabolism / Lipids / Metabolites / Microscopy / molecular biophysics / Nerve Tissue Proteins - genetics / Nerve Tissue Proteins - metabolism / Pannexin / Physiological aspects / selectivity / Signal Transduction / Spermidine / Spodoptera - genetics / Spodoptera - metabolism / Structural Biology and Molecular Biophysics / Surface active agents / Xenopus - genetics / Xenopus - metabolism / Xenopus Proteins - genetics / Xenopus Proteins - metabolism

2021

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ATP and large signaling metabolites flux through caspase-activated Pannexin 1 channels

2021

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2021

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Journal Article

ATP and large signaling metabolites flux through caspase-activated Pannexin 1 channels

Gaete, Pablo S,

Contreras, Jorge E,

Oleniacz, Patrycja W,

Medina, Christopher B,

Jin, Xueyao,

Narahari, Adishesh K,

Barrett, Paula Q,

Kiessling, Volker,

Bayliss, Douglas A,

Leonhardt, Susan A,

Yeager, Mark,

Tamm, Lukas K,

Ravichandran, Kodi S,

Kreutzberger, Alex JB,

Chiu, Yu-Hsin

2021

Overview

Pannexin 1 (Panx1) is a membrane channel implicated in numerous physiological and pathophysiological processes via its ability to support release of ATP and other cellular metabolites for local intercellular signaling. However, to date, there has been no direct demonstration of large molecule permeation via the Panx1 channel itself, and thus the permselectivity of Panx1 for different molecules remains unknown. To address this, we expressed, purified, and reconstituted Panx1 into proteoliposomes and demonstrated that channel activation by caspase cleavage yields a dye-permeable pore that favors flux of anionic, large-molecule permeants (up to ~1 kDa). Large cationic molecules can also permeate the channel, albeit at a much lower rate. We further show that Panx1 channels provide a molecular pathway for flux of ATP and other anionic (glutamate) and cationic signaling metabolites (spermidine). These results verify large molecule permeation directly through caspase-activated Panx1 channels that can support their many physiological roles.

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Publisher

eLife Science Publications, Ltd,eLife Sciences Publications Ltd,eLife Sciences Publications, Ltd

Subject

Adenosine Triphosphate - metabolism

/ Animals

/ Apoptosis

/ Caspase

/ Caspases - metabolism

/ Chromatography

/ Connexins - genetics