scholarly journals Transduction of mechanical cellular oscillation by the plasma-membrane mechanosensitive channel MSL10

2019 ◽  
Author(s):  
Daniel Tran ◽  
Tiffanie Girault ◽  
Marjorie Guichard ◽  
Sébastien Thomine ◽  
Nathalie Leblanc-Fournier ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Protein Complexes ◽  
Electrical Signal ◽  
Mechanosensitive Channel ◽  
Efficient System ◽  
Universal System ◽  
Thermal Exchange ◽  
Model Plant Arabidopsis Thaliana ◽  
Membrane Stretching ◽  
Open Question

AbstractThroughout their life, plants are submitted to recurrent cyclic mechanical loading due to wind. The resulting passive oscillation movements of stem and foliage is an important phenomenon for biological and ecological issues such as photosynthesis optimization 1–3 and thermal exchange 4. The induced motions at plant scale are well described and analyzed, with oscillations at typically 1 to 3 Hz in trees 5–10. However, the cellular perception and transduction of such recurring mechanical signals remains an open question. Multimeric protein complexes forming mechanosensitive (MS) channels embedded in the membrane provide an efficient system to rapidly convert mechanical tension into electrical signal 11. Here we show that the plasma membrane mechanosensitive channel MscS-LIKE 10 (MSL10) from the model plant Arabidopsis thaliana responds to pulsed membrane stretching with rapid activation and relaxation kinetics in the range of one second. Under sinusoidal membrane stretching MSL10 presents a greater activity than under static stimulation and behaves as a large bandpass oscillation “follower” without filtering the signal in the range of 0.3 to 3 Hz. With a localization in aerial organs naturally submitted to oscillations, our results suggest that the mechanosensitive channel MSL10 represents a molecular component of a universal system of oscillatory perception in plants.

scholarly journals Cellular transduction of mechanical oscillations in plants by the plasma-membrane mechanosensitive channel MSL10

2020 ◽  
Vol 118 (1) ◽  
pp. e1919402118
Author(s):  
Daniel Tran ◽  
Tiffanie Girault ◽  
Marjorie Guichard ◽  
Sébastien Thomine ◽  
Nathalie Leblanc-Fournier ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Protein Complexes ◽  
Electrical Signal ◽  
Efficient System ◽  
Mechanical Oscillations ◽  
Multimeric Protein ◽  
Membrane Stretching ◽  
Static Conditions ◽  
Open Question ◽  
Rapid Activation

Plants spend most of their life oscillating around 1–3 Hz due to the effect of the wind. Therefore, stems and foliage experience repetitive mechanical stresses through these passive movements. However, the mechanism of the cellular perception and transduction of such recurring mechanical signals remains an open question. Multimeric protein complexes forming mechanosensitive (MS) channels embedded in the membrane provide an efficient system to rapidly convert mechanical tension into an electrical signal. So far, studies have mostly focused on nonoscillatory stretching of these channels. Here, we show that the plasma-membrane MS channel MscS-LIKE 10 (MSL10) from the model plant Arabidopsis thaliana responds to pulsed membrane stretching with rapid activation and relaxation kinetics in the range of 1 s. Under sinusoidal membrane stretching MSL10 presents a greater activity than under static stimulation. We observed this amplification mostly in the range of 0.3–3 Hz. Above these frequencies the channel activity is very close to that under static conditions. With a localization in aerial organs naturally submitted to wind-driven oscillations, our results suggest that the MS channel MSL10, and by extension MS channels sharing similar properties, represents a molecular component allowing the perception of oscillatory mechanical stimulations by plants.

scholarly journals Free diffusion of PI(4,5)P2 in the plasma membrane in the presence of high density effector protein complexes

2022 ◽  
Author(s):  
Jonathan Pacheco ◽  
Anna C Cassidy ◽  
James P Zewe ◽  
Rachel C Wills ◽  
Gerald R Hammond
Keyword(s):  
Plasma Membrane ◽  
Protein Complexes ◽  
Focal Adhesions ◽  
Single Particle Tracking ◽  
Effector Proteins ◽  
Coated Pits ◽  
Single Class ◽  
And Function ◽  
Cytoskeletal Elements ◽  
Open Question

The lipid phosphatidyl-D-myo-inositol-4,5-bisphosphate [PI(4,5)P2] is a master regulator of plasma membrane (PM) function. It engages effector proteins that regulate diverse traffic, transport, signaling and cytoskeletal processes that define PM structure and function. How a single class of lipid molecules independently regulate so many parallel processes remains an open question. We tested the hypothesis that spatially segregated pools of PI(4,5)P2 are associated with, and thus reserved for regulation of, different functional complexes in the PM. The mobility of PI(4,5)P2 in the membrane was measured using lipid biosensors by single particle tracking photoactivation localization microscopy (sptPALM). We found that PI(4,5)P2, and several other classes of inner PM lipids, diffuse rapidly at approximately 0.3 microns squared per second with largely Brownian motion, although they spend approximately a third of their time diffusing much more slowly. Surprisingly, areas of the PM occupied by PI(4,5)P2-dependent complexes, such endoplasmic-reticulum:PM contact sites, clathrin-coated structures, and several actin cytoskeletal elements including focal adhesions, did not cause a change in PI(4,5)P2 lateral mobility. Only the spectrin and septin cytoskeletons were observed to produce a slowing of PI(4,5)P2 diffusion. We conclude that even structures with high densities of PI(4,5)P2-engaging effector proteins, such as clathrin coated pits and focal adhesions, do not corral free PI(4,5)P2, questioning a role for spatially segregated PI(4,5)P2 pools in organizing and regulating parallel PM functions.

scholarly journals Probing the biogenesis pathway and dynamics of thylakoid membranes

2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Tuomas Huokko ◽  
Tao Ni ◽  
Gregory F. Dykes ◽  
Deborah M. Simpson ◽  
Philip Brownridge ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Photosystem I ◽  
Spatial Organization ◽  
Electron Flux ◽  
Protein Complexes ◽  
Thylakoid Membranes ◽  
Thylakoid Biogenesis ◽  
Photosynthetic Complexes ◽  
Photosynthetic Machinery ◽  
Pcc 7942

AbstractHow thylakoid membranes are generated to form a metabolically active membrane network and how thylakoid membranes orchestrate the insertion and localization of protein complexes for efficient electron flux remain elusive. Here, we develop a method to modulate thylakoid biogenesis in the rod-shaped cyanobacterium Synechococcus elongatus PCC 7942 by modulating light intensity during cell growth, and probe the spatial-temporal stepwise biogenesis process of thylakoid membranes in cells. Our results reveal that the plasma membrane and regularly arranged concentric thylakoid layers have no physical connections. The newly synthesized thylakoid membrane fragments emerge between the plasma membrane and pre-existing thylakoids. Photosystem I monomers appear in the thylakoid membranes earlier than other mature photosystem assemblies, followed by generation of Photosystem I trimers and Photosystem II complexes. Redistribution of photosynthetic complexes during thylakoid biogenesis ensures establishment of the spatial organization of the functional thylakoid network. This study provides insights into the dynamic biogenesis process and maturation of the functional photosynthetic machinery.

scholarly journals Three wall-associated kinases required for rice basal immunity form protein complexes in the plasma membrane

2016 ◽  
Vol 11 (4) ◽  
pp. e1149676 ◽  
Author(s):  
Bastien Cayrol ◽  
Amandine Delteil ◽  
Enrico Gobbato ◽  
Thomas Kroj ◽  
Jean-Benoit Morel
Keyword(s):  
Plasma Membrane ◽  
Protein Complexes ◽  
Basal Immunity

scholarly journals Periprotein lipidomes of Saccharomyces cerevisiae provide a flexible environment for conformational changes of membrane proteins

eLife ◽  
2020 ◽  
Vol 9 ◽  
Author(s):  
Joury S van 't Klooster ◽  
Tan-Yun Cheng ◽  
Hendrik R Sikkema ◽  
Aike Jeucken ◽  
Branch Moody ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Membrane Proteins ◽  
Small Molecules ◽  
Conformational Changes ◽  
Direct Detection ◽  
Protein Complexes ◽  
Lateral Diffusion ◽  
Low Ph ◽  
Lipid Particles ◽  
High Degree

Yeast tolerates a low pH and high solvent concentrations. The permeability of the plasma membrane (PM) for small molecules is low and lateral diffusion of proteins is slow. These findings suggest a high degree of lipid order, which raises the question of how membrane proteins function in such an environment. The yeast PM is segregated into the Micro-Compartment-of-Can1 (MCC) and Pma1 (MCP), which have different lipid compositions. We extracted proteins from these microdomains via stoichiometric capture of lipids and proteins in styrene-maleic-acid-lipid-particles (SMALPs). We purified SMALP-lipid-protein complexes by chromatography and quantitatively analyzed periprotein lipids located within the diameter defined by one SMALP. Phospholipid and sterol concentrations are similar for MCC and MCP, but sphingolipids are enriched in MCP. Ergosterol is depleted from this periprotein lipidome, whereas phosphatidylserine is enriched relative to the bulk of the plasma membrane. Direct detection of PM lipids in the 'periprotein space' supports the conclusion that proteins function in the presence of a locally disordered lipid state.

scholarly journals Synergistic Assembly of Linker for Activation of T Cells Signaling Protein Complexes in T Cell Plasma Membrane Domains

2003 ◽  
Vol 278 (22) ◽  
pp. 20389-20394 ◽  
Author(s):  
Lorian C. Hartgroves ◽  
Joseph Lin ◽  
Hanno Langen ◽  
Tobias Zech ◽  
Arthur Weiss ◽  
...  
Keyword(s):  
T Cells ◽  
Plasma Membrane ◽  
T Cell ◽  
Protein Complexes ◽  
Membrane Domains ◽  
Cell Plasma Membrane ◽  
Signaling Protein ◽  
Cell Plasma ◽  
Plasma Membrane Domains

scholarly journals ATP- and Cytosol-dependent Release of Adaptor Proteins from Clathrin-coated Vesicles: A Dual Role for Hsc70

1998 ◽  
Vol 9 (8) ◽  
pp. 2217-2229 ◽  
Author(s):  
Lisa A. Hannan ◽  
Sherri L. Newmyer ◽  
Sandra L. Schmid
Keyword(s):  
Plasma Membrane ◽  
Protein Complexes ◽  
Adaptor Protein ◽  
Adaptor Proteins ◽  
Dual Role ◽  
Vesicular Trafficking ◽  
Coated Vesicles ◽  
Golgi Network ◽  
Cytosolic Factor

Clathrin-coated vesicles (CCV) mediate protein sorting and vesicular trafficking from the plasma membrane and the trans-Golgi network. Before delivery of the vesicle contents to the target organelles, the coat components, clathrin and adaptor protein complexes (APs), must be released. Previous work has established that hsc70/the uncoating ATPase mediates clathrin release in vitro without the release of APs. AP release has not been reconstituted in vitro, and nothing is known about the requirements for this reaction. We report a novel quantitative assay for the ATP- and cytosol- dependent release of APs from CCV. As expected, hsc70 is not sufficient for AP release; however, immunodepletion and reconstitution experiments establish that it is necessary. Interestingly, complete clathrin release is not a prerequisite for AP release, suggesting that hsc70 plays a dual role in recycling the constituents of the clathrin coat. This assay provides a functional basis for identification of the additional cytosolic factor(s) required for AP release.

A review on mmWave based energy efficient RoF system for next generation mobile communication and broadband systems

2021 ◽  
Vol 0 (0) ◽  
Author(s):  
Parvin Kumar ◽  
Sanjay Kumar Sharma ◽  
Shelly Singla ◽  
Varun Gupta ◽  
Abhishek Sharma
Keyword(s):  
Wireless Communication ◽  
Optical Fiber ◽  
Millimeter Wave ◽  
Mobile Communication ◽  
Energy Efficient ◽  
Mobile Station ◽  
Base Station ◽  
Electrical Signal ◽  
Next Generation ◽  
Efficient System

Abstract In today’s scenario, wireless communication is turning into a decisive and leading backbone to access the worldwide network. Therefore, the usage of mobile phones and broadband is rising staggeringly. To satisfy their expulsive needs, it demands increment in data rates while providing higher bandwidth and utilizing optical fiber in wireless communication, and this becomes a worldwide analysis area. Radio over fiber (RoF) system is taken into account as best solution to fulfill these needs. In RoF system, the radio frequency signal operated at millimeter wave (30–300 GHz) is centralized and processed at control station (CS) and also, the CS upconverts this electrical signal to optical domain. By employing optical fiber link, this signal reaches to base station (BS). Then, the received optical signal converts back to electrical domain at the respective BS. Now BS radiates the electrical signal to corresponding mobile station (MS) in commission with the millimeter wave frequency bands. This RoF system is providing massive bandwidth, facilitating large mobility for RF frequency signals, small loss, fast and cost effective setup, wonderful security, and unlicensed spectrum etc. The RoF system introduces microcells structure for BS cells to boost the frequency reuse and needed capacity. It has benefits in terms of ability to fulfill increasing bandwidth demands to cut back the power consumption and the dimensions of the handset devices. This paper firstly explains the overview of existing wireless mobile communication and broadband systems and then, targets the review of RoF system which will become energy efficient system for next generation mobile communication and future broadband systems. This paper also includes the performance degradation and evaluation parameters. Finally, this paper presents the various research opportunities for its implementation zone.

Temperature-sensitive mutants of MscL mechanosensitive channel

2019 ◽  
Vol 166 (3) ◽  
pp. 281-288 ◽  
Author(s):  
Naoto Owada ◽  
Megumi Yoshida ◽  
Kohei Morita ◽  
Kenjiro Yoshimura
Keyword(s):  
Escherichia Coli ◽  
Amino Acids ◽  
Structural Change ◽  
Cell Growth ◽  
Thermodynamic Stability ◽  
Transmembrane Helix ◽  
Mechanosensitive Channel ◽  
Temperature Sensitive ◽  
Temperature Sensitive Mutants ◽  
Membrane Stretching

Abstract MscL is a mechanosensitive channel that undergoes a global conformational change upon application of membrane stretching. To elucidate how the structural stability and flexibility occur, we isolated temperature-sensitive (Ts) mutants of Escherichia coli MscL that allowed cell growth at 32°C but not at 42°C. Two Ts mutants, L86P and D127V, were identified. The L86P mutation occurred in the second transmembrane helix, TM2. Substitution of residues neighbouring L86 with proline also led to a Ts mutation, but the substitution of L86 with other amino acids did not result in a Ts phenotype, indicating that the Ts phenotype was due to a structural change of TM2 helix by the introduction of a proline residue. The D127V mutation was localized in the electrostatic belt of the bundle of cytoplasmic helices, indicating that stability of the pentameric bundle of the cytoplasmic helix affects MscL structure. Together, this study described a novel class of MscL mutations that were correlated with the thermodynamic stability of the MscL structure.

Sign in / Sign up

Export Citation Format

Share Document