scholarly journals Active diffusion and advection in theDrosophilaooplasm result from the interplay of the actin and microtubule cytoskeletons

2017 ◽  
Author(s):  
Maik Drechsler ◽  
Fabio Giavazzi ◽  
Roberto Cerbino ◽  
Isabel M. Palacios

ABSTRACTTransport in cells occurs via a delicate interplay of passive and active processes, including diffusion, directed transport and advection. Despite progresses in super-resolution microscopy, discriminating and quantifying these processes is a challenge, requiring tracking of rapidly moving, sub-diffraction objects in a crowded, noisy environment. Here we use Differential Dynamic Microscopy with different contrast mechanisms to provide a thorough characterization of the dynamics in theDrosophilaoocyte. We study the movement of vesicles and the elusive motion of a cytoplasmic F-actin mesh, a known regulator of cytoplasmic flows. We find that cytoplasmic motility constitutes a combination of directed motion and random diffusion. While advection is mainly attributed to microtubules, we find that active diffusion is driven by the actin cytoskeleton, although it is also enhanced by the flow. We also find that an important dynamic link exists between vesicles and cytoplasmic F-actin motion, as recently suggested in mouse oocytes.

2017 ◽  
Vol 56 (22) ◽  
pp. 6131-6135 ◽  
Author(s):  
Anne Burgert ◽  
Jan Schlegel ◽  
Jérôme Bécam ◽  
Sören Doose ◽  
Erhard Bieberich ◽  
...  

2021 ◽  
Author(s):  
Lisa A.E. Catsburg ◽  
Manon Westra ◽  
Annemarie M. L. van Schaik ◽  
Harold D. MacGillavry

ABSTRACTAt postsynaptic sites of neurons, a prominent clathrin-coated structure, the endocytic zone (EZ), controls the trafficking of glutamate receptors and is essential for synaptic plasticity. Despite its importance, little is known about how this clathrin structure is organized to mediate endocytosis. We used live-cell and super-resolution microscopy techniques to reveal the dynamic organization of this poorly understood clathrin structure. We found that a subset of endocytic proteins only transiently appeared at postsynaptic sites. In contrast, other proteins, including Eps15, intersectin1L, and β2-adaptin, were persistently enriched and partitioned at the edge of the EZ. We found that uncoupling the EZ from the synapse led to the loss of most of these components, while disrupting the actin cytoskeleton or AP2-membrane interactions did not alter EZ positioning. We conclude that the EZ is a stable, highly organized molecular platform where components are differentially recruited and positioned to orchestrate the endocytosis of synaptic receptors.


2021 ◽  
Author(s):  
Shikha Dhiman ◽  
Teodora Andrian ◽  
Beatriz Santiago ◽  
Marrit Tholen ◽  
Yuyang Wang ◽  
...  

The characterization of newly synthesized materials is a cornerstone of all chemistry and nanotechnology laboratories. For this purpose, a wide array of analytical techniques have been standardized and are used...


2009 ◽  
Vol 17 (10) ◽  
pp. 8264 ◽  
Author(s):  
Michael J. Mlodzianoski ◽  
Manuel F. Juette ◽  
Glen L. Beane ◽  
Joerg Bewersdorf

2017 ◽  
Vol 112 (3) ◽  
pp. 148a
Author(s):  
Elizabeth M. Smith ◽  
Ragnar Stefansson ◽  
Maria Paz Ramirez Lopez ◽  
Elias M. Puchner

Author(s):  
Maria Arista-Romero ◽  
Silvia Pujals ◽  
Lorenzo Albertazzi

In the last year the COVID19 pandemic clearly illustrated the potential threat that viruses pose to our society. The characterization of viral structures and the identification of key proteins involved in each step of the cycle of infection are crucial to develop treatments. However, the small size of viruses, invisible under conventional fluorescence microscopy, make it difficult to study the organization of protein clusters within the viral particle. The applications of super-resolution microscopy have skyrocketed in the last years, converting this group into one of the leading techniques to characterize viruses and study the viral infection in cells, breaking the diffraction limit by achieving resolutions up to 10 nm using conventional probes such as fluorescent dyes and proteins. There are several super-resolution methods available and the selection of the right one it is crucial to study in detail all the steps involved in the viral infection, quantifying and creating models of infection for relevant viruses such as HIV-1, Influenza, herpesvirus or SARS-CoV-1. Here we review the use of super-resolution microscopy (SRM) to study all steps involved in the viral infection and antiviral design. In light of the threat of new viruses, these studies could inspire future assays to unveil the viral mechanism of emerging viruses and further develop successful antivirals against them.


2019 ◽  
Author(s):  
Cristina Bertocchi ◽  
Andrea Ravasio ◽  
Hui Ting Ong ◽  
Yusuke Toyama ◽  
Pakorn Kanchanawong

SummaryMechanical force transmission through the adherens junctions (AJs) are highly regulated processes essential for multicellular organization of tissues. AJ proteins such as E-cadherin, α-catenin, and vinculin have been shown to be sensing or bearing mechanical forces being transmitted between the actin cytoskeleton and the intercellular contacts. However, the molecular organization and connectivity of these components remains not well understood. Using a super-resolution microscopy approach, we report that vinculin, once activated, could form a direct structural connection with β-catenin, which can bypass α-catenin, one of the main mechanotransducers in AJs. Direct vinculin/β-catenin interaction is capable of supporting mechanical tension and contributes to the stabilization of the cadherin-catenin complexes. These findings suggest a multi-step model for the force-dependent reinforcement of AJs whereby α-catenin may serve as the initial catalytic activator of vinculin, followed by vinculin translocation to form a direct link between E-cadherin-bound β-catenin and the actin cytoskeleton.


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