How cells channel their stress: Interplay between Piezo1 and the cytoskeleton

Nourse, Jamie P.; Pathak, Madhu A.

doi:10.1016/j.semcdb.2017.06.018

Cited by 187 publications

(199 citation statements)

References 75 publications

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“…Indeed, a mechanically-activated protein has recently been shown to have a more expanded constriction pore in the presence of a positive mismatch (thicker lipids) than in negative mismatch (thinner lipids) [62]. Third, GM1-enriched domains appear dependent on the anchorage through ankyrin (our unpublished data) and the cytoskeleton is known to modulate Piezo1 activity [63].…”

Section: Lipid Domains As Modulators Of Piezo1 and Pmca Membrane Locamentioning

confidence: 73%

Spatial Relationship and Functional Relevance of Three Lipid Domain Populations at the Erythrocyte Surface

Conrard

Stommen

Cloos

et al. 2018

Cell Physiol Biochem

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Background/Aims: Red blood cells (RBC) have been shown to exhibit stable submicrometric lipid domains enriched in cholesterol (chol), sphingomyelin (SM), phosphatidylcholine (PC) or ganglioside GM1, which represent the four main lipid classes of their outer plasma membrane leaflet. However, whether those lipid domains co-exist at the RBC surface or are spatially related and whether and how they are subjected to reorganization upon RBC deformation are not known. Methods: Using fluorescence and/or confocal microscopy and well-validated probes, we compared these four lipid-enriched domains for their abundance, curvature association, lipid order, temperature dependence, spatial dissociation and sensitivity to RBC mechanical stimulation. Results: Our data suggest that three populations of lipid domains with decreasing abundance coexist at the RBC surface: (i) chol-enriched ones, associated with RBC high curvature areas; (ii) GM1/PC/chol-enriched ones, present in low curvature areas; and (iii) SM/PC/chol-enriched ones, also found in low curvature areas. Whereas chol-enriched domains gather in increased curvature areas upon RBC deformation, low curvature-associated lipid domains increase in abundance either upon calcium influx during RBC deformation (GM1/PC/chol-enriched domains) or upon secondary calcium efflux during RBC shape restoration (SM/PC/chol-enriched domains). Hence, abrogation of these two domain populations is accompanied by a strong impairment of the intracellular calcium balance. Conclusion: Lipid domains could contribute to calcium influx and efflux by controlling the membrane distribution and/or the activity of the mechano-activated ion channel Piezo1 and the calcium pump PMCA. Whether this results from lipid domain biophysical properties, the strength of their anchorage to the underlying cytoskeleton and/or their correspondence with inner plasma membrane leaflet lipids remains to be demonstrated.

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Section: Lipid Domains As Modulators Of Piezo1 and Pmca Membrane Locamentioning

confidence: 73%

Spatial Relationship and Functional Relevance of Three Lipid Domain Populations at the Erythrocyte Surface

Conrard

Stommen

Cloos

et al. 2018

Cell Physiol Biochem

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“…McHugh et al (2010) have shown that Piezo1 channels localize to the endoplasmic reticulum (ER) in epithelial cells where they can regulate integrin-mediated cell adhesion via calpain and talin activation. Therefore, Piezo1 channels can regulate intracellular Ca 2+ concentrations via Ca 2+ release from intracellular stores or through the formation of mechanically-gated ion channels in the outer cell membrane (Nourse & Pathak, 2017). Interestingly, Piezo1 is also voltage sensitive (Moroni, Servin-Vences, Fleischer, Sanchez-Carranza, & Lewin, 2018) and, therefore, its repertoire of known functions in CNS neurons and glial cells, both in health and disease, is likely to increase in the near future.…”

Section: Introductionmentioning

confidence: 99%

Piezo1 regulates calcium oscillations and cytokine release from astrocytes

Velasco‐Estevez

Rolle

Mampay

et al. 2019

Glia

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Astrocytes are important for information processing in the brain and they achieve this by fine‐tuning neuronal communication via continuous uptake and release of biochemical modulators of neurotransmission and synaptic plasticity. Often overlooked are their important functions in mechanosensation. Indeed, astrocytes can detect pathophysiological changes in the mechanical properties of injured, ageing, or degenerating brain tissue. We have recently shown that astrocytes surrounding mechanically‐stiff amyloid plaques upregulate the mechanosensitive ion channel, Piezo1. Moreover, ageing transgenic Alzheimer's rats harboring a chronic peripheral bacterial infection displayed enhanced Piezo1 expression in amyloid plaque‐reactive astrocytes of the hippocampus and cerebral cortex. Here, we have shown that the bacterial endotoxin, lipopolysaccharide (LPS), also upregulates Piezo1 in primary mouse cortical astrocyte cultures in vitro. Activation of Piezo1, via the small molecule agonist Yoda1, enhanced Ca2+ influx in both control and LPS‐stimulated astrocytes. Moreover, Yoda1 augmented intracellular Ca2+ oscillations but decreased subsequent Ca2+ influx in response to adenosine triphosphate (ATP) stimulation. Neither blocking nor activating Piezo1 affected cell viability. However, LPS‐stimulated astrocyte cultures exposed to the Piezo1 activator, Yoda1, migrated significantly slower than reactive astrocytes treated with the mechanosensitive channel‐blocking peptide, GsMTx4. Furthermore, our data show that activating Piezo1 channels inhibits the release of cytokines and chemokines, such as IL‐1β, TNFα, and fractalkine (CX3CL1), from LPS‐stimulated astrocyte cultures. Taken together, our results suggest that astrocytic Piezo1 upregulation may act to dampen neuroinflammation and could be a useful drug target for neuroinflammatory disorders of the brain.

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“…This is supported by biophysical studies that Piezo1 is sensitive to specific lipid types 14 and the observations that Piezo1 is diffusively localized in plasma membranes of many cell lines with very few interaction partners identified 4,13,15,16 . However, an open question In the regulation of Piezo1 is the intimate involvement of the integrin-linked actin cytoskeleton in Piezo1's functions 17 . Before the discovery of Piezo1 as a mechanosensitive ion channel, Piezo1 was shown to be involved in integrin activation 18 .…”

Section: Introductionmentioning

confidence: 99%

Force-dependent recruitment of Piezo1 drives adhesion maturation and calcium entry in normal but not tumor cells

Yao

Tijore

Cox

et al. 2020

Preprint

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Piezo1 is a mechanosensitive Ca 2+ -permeable channel that has been implicated in a number of mechanosensing processes. It is diffusive on plasma membranes and activated by local membrane tension changes yet recent data suggest that Piezo1 activity is tightly coupled to the integrin-mediated actin cytoskeleton through a poorly understood mechanism. In our studies, we found that Piezo1 stably localizes to RGD matrix adhesions in normal but not in transformed cells. Piezo1 binding requires contractility and triggers local Ca 2+ entry during adhesion formation and turnover. In transformed cells, Piezo1 level does not affect adhesion morphology; and there is no detectable Ca 2+ influx around adhesions. Based upon these findings, we suggest that Piezo1 is a novel component of integrin-based adhesions in non-transformed cells and contributes to the distinct mechanosensing and Ca 2+ signaling in normal vs transformed cells.Concentration of Piezo1 at adhesions is a key factor underlying Piezo1's physiological functions.

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How cells channel their stress: Interplay between Piezo1 and the cytoskeleton

Cited by 187 publications

References 75 publications

Spatial Relationship and Functional Relevance of Three Lipid Domain Populations at the Erythrocyte Surface

Spatial Relationship and Functional Relevance of Three Lipid Domain Populations at the Erythrocyte Surface

Piezo1 regulates calcium oscillations and cytokine release from astrocytes

Force-dependent recruitment of Piezo1 drives adhesion maturation and calcium entry in normal but not tumor cells

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