The Pannexin1 membrane channel: distinct conformations and functions

Research output: Contribution to journalReview article

4 Citations (Scopus)

Abstract

The Pannexin1 (Panx1) membrane channel responds to different stimuli with distinct channel conformations. Most stimuli induce a large cation- and ATP-permeable conformation, hence Panx1 is involved in many physiological processes entailing purinergic signaling. For example, oxygen delivery in the peripheral circulatory system is regulated by ATP released from red blood cells and endothelial cells through Panx1 channels. The same membrane channel, however, when stimulated by positive membrane potential or by cleavage with caspase 3, is highly selective for the passage of chloride ions, excluding cations and ATP. Although biophysical data do not allow a distinction between the chloride-selective channels induced by voltage or by caspase cleavage, there must be other subtle differences in the structure, because overexpression of wtPanx1 is well tolerated by cells, while expression of the truncation mutant Panx1Δ378 results in slow cell death. Thus, in addition to the well-characterized two open conformations, there might be a third, more subtle conformational change involved in cell death.

Original languageEnglish (US)
Pages (from-to)3201-3209
Number of pages9
JournalFEBS Letters
Volume592
Issue number19
DOIs
StatePublished - Oct 1 2018

Fingerprint

Ion Channels
Conformations
Adenosine Triphosphate
Cell death
Cations
Chlorides
Cell Death
Physiological Phenomena
Chloride Channels
Endothelial cells
Caspases
Cardiovascular System
Caspase 3
Membrane Potentials
Blood
Endothelial Cells
Erythrocytes
Cells
Ions
Oxygen

Keywords

  • amplification
  • ATP
  • caspase
  • cation
  • Pannexin
  • permeability
  • potassium
  • selectivity

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

Cite this

The Pannexin1 membrane channel : distinct conformations and functions. / Dahl, Gerhard.

In: FEBS Letters, Vol. 592, No. 19, 01.10.2018, p. 3201-3209.

Research output: Contribution to journalReview article

@article{2c0f89f8961748a49c9a53d128999fd2,
title = "The Pannexin1 membrane channel: distinct conformations and functions",
abstract = "The Pannexin1 (Panx1) membrane channel responds to different stimuli with distinct channel conformations. Most stimuli induce a large cation- and ATP-permeable conformation, hence Panx1 is involved in many physiological processes entailing purinergic signaling. For example, oxygen delivery in the peripheral circulatory system is regulated by ATP released from red blood cells and endothelial cells through Panx1 channels. The same membrane channel, however, when stimulated by positive membrane potential or by cleavage with caspase 3, is highly selective for the passage of chloride ions, excluding cations and ATP. Although biophysical data do not allow a distinction between the chloride-selective channels induced by voltage or by caspase cleavage, there must be other subtle differences in the structure, because overexpression of wtPanx1 is well tolerated by cells, while expression of the truncation mutant Panx1Δ378 results in slow cell death. Thus, in addition to the well-characterized two open conformations, there might be a third, more subtle conformational change involved in cell death.",
keywords = "amplification, ATP, caspase, cation, Pannexin, permeability, potassium, selectivity",
author = "Gerhard Dahl",
year = "2018",
month = "10",
day = "1",
doi = "10.1002/1873-3468.13115",
language = "English (US)",
volume = "592",
pages = "3201--3209",
journal = "FEBS Letters",
issn = "0014-5793",
publisher = "Elsevier",
number = "19",

}

TY - JOUR

T1 - The Pannexin1 membrane channel

T2 - distinct conformations and functions

AU - Dahl, Gerhard

PY - 2018/10/1

Y1 - 2018/10/1

N2 - The Pannexin1 (Panx1) membrane channel responds to different stimuli with distinct channel conformations. Most stimuli induce a large cation- and ATP-permeable conformation, hence Panx1 is involved in many physiological processes entailing purinergic signaling. For example, oxygen delivery in the peripheral circulatory system is regulated by ATP released from red blood cells and endothelial cells through Panx1 channels. The same membrane channel, however, when stimulated by positive membrane potential or by cleavage with caspase 3, is highly selective for the passage of chloride ions, excluding cations and ATP. Although biophysical data do not allow a distinction between the chloride-selective channels induced by voltage or by caspase cleavage, there must be other subtle differences in the structure, because overexpression of wtPanx1 is well tolerated by cells, while expression of the truncation mutant Panx1Δ378 results in slow cell death. Thus, in addition to the well-characterized two open conformations, there might be a third, more subtle conformational change involved in cell death.

AB - The Pannexin1 (Panx1) membrane channel responds to different stimuli with distinct channel conformations. Most stimuli induce a large cation- and ATP-permeable conformation, hence Panx1 is involved in many physiological processes entailing purinergic signaling. For example, oxygen delivery in the peripheral circulatory system is regulated by ATP released from red blood cells and endothelial cells through Panx1 channels. The same membrane channel, however, when stimulated by positive membrane potential or by cleavage with caspase 3, is highly selective for the passage of chloride ions, excluding cations and ATP. Although biophysical data do not allow a distinction between the chloride-selective channels induced by voltage or by caspase cleavage, there must be other subtle differences in the structure, because overexpression of wtPanx1 is well tolerated by cells, while expression of the truncation mutant Panx1Δ378 results in slow cell death. Thus, in addition to the well-characterized two open conformations, there might be a third, more subtle conformational change involved in cell death.

KW - amplification

KW - ATP

KW - caspase

KW - cation

KW - Pannexin

KW - permeability

KW - potassium

KW - selectivity

UR - http://www.scopus.com/inward/record.url?scp=85054803361&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=85054803361&partnerID=8YFLogxK

U2 - 10.1002/1873-3468.13115

DO - 10.1002/1873-3468.13115

M3 - Review article

C2 - 29802622

AN - SCOPUS:85054803361

VL - 592

SP - 3201

EP - 3209

JO - FEBS Letters

JF - FEBS Letters

SN - 0014-5793

IS - 19

ER -