scholarly journals Detecting Transient Trapping from a Single Trajectory: A Structural Approach

Entropy ◽  
2021 ◽  
Vol 23 (8) ◽  
pp. 1044
Author(s):  
Yann Lanoiselée ◽  
Jak Grimes ◽  
Zsombor Koszegi ◽  
Davide Calebiro
Keyword(s):  
Plasma Membrane ◽  
Single Particle ◽  
Adrenergic Receptors ◽  
Particle Trajectory ◽  
Temporal Structure ◽  
Structural Approach ◽  
New Method ◽  
Trajectory Data ◽  
Receptor Stimulation ◽  
Over Time

In this article, we introduce a new method to detect transient trapping events within a single particle trajectory, thus allowing the explicit accounting of changes in the particle’s dynamics over time. Our method is based on new measures of a smoothed recurrence matrix. The newly introduced set of measures takes into account both the spatial and temporal structure of the trajectory. Therefore, it is adapted to study short-lived trapping domains that are not visited by multiple trajectories. Contrary to most existing methods, it does not rely on using a window, sliding along the trajectory, but rather investigates the trajectory as a whole. This method provides useful information to study intracellular and plasma membrane compartmentalisation. Additionally, this method is applied to single particle trajectory data of β2-adrenergic receptors, revealing that receptor stimulation results in increased trapping of receptors in defined domains, without changing the diffusion of free receptors.

scholarly journals Norepinephrine Protects against Methamphetamine Toxicity through β2-Adrenergic Receptors Promoting LC3 Compartmentalization

2021 ◽  
Vol 22 (13) ◽  
pp. 7232
Author(s):  
Gloria Lazzeri ◽  
Carla L. Busceti ◽  
Francesca Biagioni ◽  
Cinzia Fabrizi ◽  
Gabriele Morucci ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Light Chain ◽  
Adrenergic Receptors ◽  
Cell Damage ◽  
Protective Effects ◽  
Autophagy Flux ◽  
Brain Areas ◽  
Indirect Consequence

Norepinephrine (NE) neurons and extracellular NE exert some protective effects against a variety of insults, including methamphetamine (Meth)-induced cell damage. The intimate mechanism of protection remains difficult to be analyzed in vivo. In fact, this may occur directly on target neurons or as the indirect consequence of NE-induced alterations in the activity of trans-synaptic loops. Therefore, to elude neuronal networks, which may contribute to these effects in vivo, the present study investigates whether NE still protects when directly applied to Meth-treated PC12 cells. Meth was selected based on its detrimental effects along various specific brain areas. The study shows that NE directly protects in vitro against Meth-induced cell damage. The present study indicates that such an effect fully depends on the activation of plasma membrane β2-adrenergic receptors (ARs). Evidence indicates that β2-ARs activation restores autophagy, which is impaired by Meth administration. This occurs via restoration of the autophagy flux and, as assessed by ultrastructural morphometry, by preventing the dissipation of microtubule-associated protein 1 light chain 3 (LC3) from autophagy vacuoles to the cytosol, which is produced instead during Meth toxicity. These findings may have an impact in a variety of degenerative conditions characterized by NE deficiency along with autophagy impairment.

scholarly journals Molecular architecture of the endocytic TPLATE complex

2021 ◽  
Vol 7 (9) ◽  
pp. eabe7999
Author(s):  
Klaas Yperman ◽  
Jie Wang ◽  
Dominique Eeckhout ◽  
Joanna Winkler ◽  
Lam Dai Vu ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Structural Approach ◽  
Eukaryotic Cells ◽  
Molecular Architecture ◽  
Membrane Proteome ◽  
Complex Assembly ◽  
Membrane Interaction ◽  
Structural Insight ◽  
Fresh Insight ◽  
Insight Into

Eukaryotic cells rely on endocytosis to regulate their plasma membrane proteome and lipidome. Most eukaryotic groups, except fungi and animals, have retained the evolutionary ancient TSET complex as an endocytic regulator. Unlike other coatomer complexes, structural insight into TSET is lacking. Here, we reveal the molecular architecture of plant TSET [TPLATE complex (TPC)] using an integrative structural approach. We identify crucial roles for specific TSET subunits in complex assembly and membrane interaction. Our data therefore generate fresh insight into the differences between the hexameric TSET in Dictyostelium and the octameric TPC in plants. Structural elucidation of this ancient adaptor complex represents the missing piece in the coatomer puzzle and vastly advances our functional as well as evolutionary insight into the process of endocytosis.

Fishing on floating objects (FOBs): how French tropical tuna purse seiners split fishing effort between GPS-monitored and unmonitored FOBs

2018 ◽  
Vol 75 (11) ◽  
pp. 1849-1858 ◽  
Author(s):  
Julia E. Snouck-Hurgronje ◽  
David M. Kaplan ◽  
Emmanuel Chassot ◽  
Alexandra Maufroy ◽  
Daniel Gaertner
Keyword(s):  
Search Time ◽  
Fishing Effort ◽  
Purse Seine ◽  
Trajectory Data ◽  
Catch Per Unit Effort ◽  
Position Information ◽  
Foreign Objects ◽  
Tropical Tuna ◽  
Floating Objects ◽  
Over Time

Fishing on floating objects (FOBs) dominates catch in tropical tuna purse seine fisheries. One frequently cited advantage of deploying GPS-monitored FOBs is that the position information can be used for directed fishing to reduce search time for tuna. However, purse seiners also fish on foreign objects for which position information is not available. It is critical to quantify the prevalence of fishing on GPS-monitored versus unmonitored FOBs to understand how they impact fishing effort and catch per unit effort. We analyzed French commercial, observer, and FOB trajectory data in the Atlantic and Indian oceans to determine how often purse seine vessels fish on GPS-monitored FOBs. Only 2.7%–20.4% of French FOB fishing sets over 2007–2013 in both oceans were made on GPS-monitored FOBs. Though increasing over time, the low percentage suggests that French vessels do not primarily use GPS-monitored FOBs to reduce search time for tuna. We hypothesize that fishery-wide FOB deployments have important collective consequences for overall fishing effort and recommend that future effort metrics should be based on fishery-wide FOB activities.

scholarly journals 2-Aminoindan and its ring-substituted derivatives interact with plasma membrane monoamine transporters and α2-adrenergic receptors

2019 ◽  
Vol 236 (3) ◽  
pp. 989-999 ◽  
Author(s):  
Adam L. Halberstadt ◽  
Simon D. Brandt ◽  
Donna Walther ◽  
Michael H. Baumann
Keyword(s):  
Plasma Membrane ◽  
Adrenergic Receptors ◽  
Monoamine Transporters

Beta-adrenergic modulation of insulin binding in skeletal muscle

1986 ◽  
Vol 250 (2) ◽  
pp. E198-E204
Author(s):  
B. Webster ◽  
S. R. Vigna ◽  
T. Paquette ◽  
D. J. Koerker
Keyword(s):  
Skeletal Muscle ◽  
Plasma Membrane ◽  
Protein Phosphatase ◽  
Adrenergic Receptors ◽  
Plasma Membranes ◽  
Acute Exercise ◽  
Insulin Binding ◽  
Beta Adrenergic Receptors ◽  
Beta Adrenergic ◽  
Adrenergic Antagonist

Both a high physiological concentration (13.1 nM) of epinephrine (E) and acute exercise (AEx) have previously been shown to increase 125I-insulin binding in skeletal muscle. To investigate the site and mechanism of the effect of epinephrine on binding and the possible link between epinephrine- and AEx-enhanced insulin binding, we measured insulin binding in three different preparations: 1) crude membranes derived from whole soleus muscle incubated in vitro with 13.1 nM E, 2) crude membranes with E present in the binding assay, and 3) purified plasma membranes with E present. Epinephrine enhanced binding in all three preparations by 169, 144, and 164%, respectively, at low concentrations of insulin but had little effect at high concentrations. Epinephrine, therefore appears to have its effect at the plasma membrane. Propranolol (10 microM), a beta-adrenergic antagonist, blocked E-enhanced insulin binding and when added to crude membranes made from soleus and extensor digitorum longus muscle of AEx rats reversed the increase in binding seen with exercise. This indicates that E-enhanced insulin binding is mediated by beta-adrenergic receptors and that AEx enhances insulin binding via beta-adrenergic receptors. Sodium orthovanadate (3 mM), a phosphotyrosyl-protein phosphatase inhibitor, also inhibited the increase in insulin binding due to E, implying that E may increase insulin binding by activating a phosphotyrosyl-protein phosphatase which decreases the phosphorylation of a plasma membrane protein, presumably the insulin receptor.

scholarly journals The cell wall regulates dynamics and size of plasma-membrane nanodomains inArabidopsis

2019 ◽  
Vol 116 (26) ◽  
pp. 12857-12862 ◽  
Author(s):  
J. F. McKenna ◽  
D. J. Rolfe ◽  
S. E. D. Webb ◽  
A. F. Tolmie ◽  
S. W. Botchway ◽  
...  
Keyword(s):  
Cell Wall ◽  
Plasma Membrane ◽  
Confocal Microscopy ◽  
Particle Tracking ◽  
Single Particle ◽  
Cluster Size ◽  
Particle Dynamics ◽  
Single Particle Tracking ◽  
Signaling Cascade ◽  
Plant Plasma Membrane

Plant plasma-membrane (PM) proteins are involved in several vital processes, such as detection of pathogens, solute transport, and cellular signaling. For these proteins to function effectively there needs to be structure within the PM allowing, for example, proteins in the same signaling cascade to be spatially organized. Here we demonstrate that several proteins with divergent functions are located in clusters of differing size in the membrane using subdiffraction-limited Airyscan confocal microscopy. Single particle tracking reveals that these proteins move at different rates within the membrane. Actin and microtubule cytoskeletons appear to significantly regulate the mobility of one of these proteins (the pathogen receptor FLS2) and we further demonstrate that the cell wall is critical for the regulation of cluster size by quantifying single particle dynamics of proteins with key roles in morphogenesis (PIN3) and pathogen perception (FLS2). We propose a model in which the cell wall and cytoskeleton are pivotal for regulation of protein cluster size and dynamics, thereby contributing to the formation and functionality of membrane nanodomains.

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