Nanosecond electric pulses trigger actin responses in plant cells

Berghöfer, Th.; Eing, C.; Flickinger, Bianca; Hohenberger, Petra; Wegner, Lars H.; Frey, Wolfgang; Nick, Peter

doi:10.1016/j.bbrc.2009.07.072

Cited by 55 publications

(43 citation statements)

References 21 publications

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“…In contrast to directly induced permeabilization, this process develops within minutes after pulse exposure. 5 In summary, the results confirm the theoretically predicted distribution of the membrane voltage for spherical cells with negligible permeabilization. The observed deviations were caused by enhanced pore formation, while the asymmetric charging process at both cell hemispheres can be explained by the high negative resting potential of plant cells.…”

Section: Discussionsupporting

confidence: 78%

Aspects of plant plasmalemma charging induced by external electric field pulses

Berghoefer

Flickinger²,

Frey³

2012

Plant Signaling & Behavior

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Section: Discussionsupporting

confidence: 78%

Aspects of plant plasmalemma charging induced by external electric field pulses

Berghoefer

Flickinger²,

Frey³

2012

Plant Signaling & Behavior

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“…Therefore, acute remodelling of actin near the site of sonoporation can by and large be regarded as a cytoprotective process that would facilitate pore closure [20,21]. In fact, a similar actin disruption phenomenon has been reported in cells punctured by a micro-tip [36] or pulsed by short-duration electrical fields [37,38].…”

Section: Accumulation Of Globular Actin In Sonoporated Cellsmentioning

confidence: 83%

Single-site sonoporation disrupts actin cytoskeleton organization

Chen

Leow

et al. 2014

J. R. Soc. Interface.

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Sonoporation is based upon an ultrasound -microbubble cavitation routine that physically punctures the plasma membrane on a transient basis. During such a process, the actin cytoskeleton may be disrupted in tandem because this network of subcellular filaments is physically interconnected with the plasma membrane. Here, by performing confocal fluorescence imaging of single-site sonoporation episodes induced by ultrasound-triggered collapse of a single targeted microbubble, we directly observed immediate rupturing of filamentary actin (F-actin) at the sonoporation site (cell type: ZR-75-30; ultrasound frequency: 1 MHz; peak negative pressure: 0.45 MPa; pulse duration: 30 cycles; bubble diameter: 2-4 mm). Also, through conducting a structure tensor analysis, we observed further disassembly of the F-actin network over the next 60 min after the onset of sonoporation. The extent of F-actin disruption was found to be more substantial in cells with higher uptake of sonoporation tracer. Commensurate with this process, cytoplasmic accumulation of globular actin (G-actin) was evident in sonoporated cells, and in turn the G-actin : F-actin ratio was increased in a trend similar to druginduced (cytochalasin D) actin depolymerization. These results demonstrate that sonoporation is not solely a membrane-level phenomenon: organization of the actin cytoskeleton is concomitantly perturbed.

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“…In such a structure, the mechanical disturbance of any individual element allows stress signals to propagate and be transduced at relatively distant locations (Ingber, 2008). Thus, the mechanically stable cell walls provide structural support, and the constant remodeling of the underlying cytoskeleton in response to mechanical disturbances acts as a tensegrity sensor (Komis et al, 2002;Berghöfer et al, 2009;Nick, 2013).…”

mentioning

confidence: 99%

The Arabidopsis Synaptotagmin1 Is Enriched in Endoplasmic Reticulum-Plasma Membrane Contact Sites and Confers Cellular Resistance to Mechanical Stresses

et al. 2015

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Eukaryotic endoplasmic reticulum (ER)-plasma membrane (PM) contact sites are evolutionarily conserved microdomains that have important roles in specialized metabolic functions such as ER-PM communication, lipid homeostasis, and Ca 2+ influx. Despite recent advances in knowledge about ER-PM contact site components and functions in yeast (Saccharomyces cerevisiae) and mammals, relatively little is known about the functional significance of these structures in plants. In this report, we characterize the Arabidopsis (Arabidopsis thaliana) phospholipid binding Synaptotagmin1 (SYT1) as a plant ortholog of the mammal extended synaptotagmins and yeast tricalbins families of ER-PM anchors. We propose that SYT1 functions at ER-PM contact sites because it displays a dual ER-PM localization, it is enriched in microtubule-depleted regions at the cell cortex, and it colocalizes with Vesicle-Associated Protein27-1, a known ER-PM marker. Furthermore, biochemical and physiological analyses indicate that SYT1 might function as an electrostatic phospholipid anchor conferring mechanical stability in plant cells. Together, the subcellular localization and functional characterization of SYT1 highlights a putative role of plant ER-PM contact site components in the cellular adaptation to environmental stresses.

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Nanosecond electric pulses trigger actin responses in plant cells

Cited by 55 publications

References 21 publications

Aspects of plant plasmalemma charging induced by external electric field pulses

Aspects of plant plasmalemma charging induced by external electric field pulses

Single-site sonoporation disrupts actin cytoskeleton organization

The Arabidopsis Synaptotagmin1 Is Enriched in Endoplasmic Reticulum-Plasma Membrane Contact Sites and Confers Cellular Resistance to Mechanical Stresses

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