Abstract

The roles of pannexin 1 (Panx1) large-pore ion and metabolite channels are becoming recognized in many physiological and pathophysiological scenarios. Recent evidence has tightly linked Panx1 trafficking and function to the cytoskeleton, a multi-component network that provides critical structural support, transportation, and scaffolding functions in all cell types. Here we review early work demonstrating the mechanosensitive activation of Panx1 channels, and expand on more recent evidence directly linking Panx1 to the cytoskeleton. Further, we examine the reciprocal regulation between Panx1 and the cytoskeleton, and discuss the involvement of Panx1 in cytoskeletal-regulated cell behaviors. Finally, we identify important gaps in the current knowledge surrounding this emerging Panx1-cytoskeleton relationship.

Highlights

  • Mechanical forces shape virtually all biological processes in myriad ways

  • Locovei et al (2006) observed that pannexin 1 (Panx1) is present in human erythrocytes, and mediates adenosine triphosphate (ATP) release and ion flux in response to depolarization and mechanical stretch elicited by pressure in the patch pipette

  • Actin-related protein 3 (Arp3), were two of several cytoskeletal proteins we recently identified as Panx1-interacting proteins by immunoprecipitation coupled to liquid chromatography and tandem mass spectrometry (LCMS/MS; Wicki-Stordeur and Swayne, 2013)

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Summary

Introduction

Mechanical forces shape virtually all biological processes in myriad ways (for a recent review see Lim et al, 2010). Panx1 has been shown to physically interact with the actin cytoskeleton (Bhalla-Gehi et al, 2010; Wicki-Stordeur and Swayne, 2013) and the expression of Panx1 exhibits a significant level of control over multiple cytoskeletal elements (Penuela et al, 2012). ACTIVATION OF Panx1 BY MECHANICAL STRESS The first demonstration of stretch-mediated Panx1 opening resulted from work in an ectopic expression system by Bao et al (2004).

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