Photoinduced Increase in Vesicle Size and Role of Photoresponsive Malachite Green Leuconitrile Derivative in Vesicle Fusion

Langmuir ◽  
2007 ◽  
Vol 23 (15) ◽  
pp. 7936-7941 ◽  
Author(s):  
Ryoko M. Uda ◽  
Daisuke Yamashita ◽  
Yoshiaki Sakurai ◽  
Keiichi Kimura
eLife ◽  
2016 ◽  
Vol 5 ◽  
Author(s):  
Wanda Kukulski ◽  
Andrea Picco ◽  
Tanja Specht ◽  
John AG Briggs ◽  
Marko Kaksonen

In a previous paper (<xref ref-type="bibr" rid="bib22">Picco et al., 2015</xref>), the dynamic architecture of the protein machinery during clathrin-mediated endocytosis was visualized using a new live imaging and particle tracking method. Here, by combining this approach with correlative light and electron microscopy, we address the role of clathrin in this process. During endocytosis, clathrin forms a cage-like coat around the membrane and associated protein components. There is growing evidence that clathrin does not determine the membrane morphology of the invagination but rather modulates the progression of endocytosis. We investigate how the deletion of clathrin heavy chain impairs the dynamics and the morphology of the endocytic membrane in budding yeast. Our results show that clathrin is not required for elongating or shaping the endocytic membrane invagination. Instead, we find that clathrin contributes to the regularity of vesicle scission and thereby to controlling vesicle size.


Author(s):  
M. A. Kupryashina ◽  
T. E. Pylaev ◽  
V. E. Nikitina

Malachite green (MG), a widely-used and recalcitrant dye, has been confirmed to be carcinogenic and mutagenic against many organisms. Herein, we were aimed at the investigation of the hypothetic role of ligninolytic bacterial enzymes similar to fungal ones in the degradation of synthetic dyes. A multiple increase in the laccases and DyP-peroxidases genes expression level was recorded by RT-qPCR for bacteria of the genus Azospirillum in the presence of MG.


2020 ◽  
Author(s):  
Rianne Grond ◽  
Tineke Veenendaal ◽  
Juan Duran ◽  
Ishier Raote ◽  
Sebastiaan Corstjens ◽  
...  

AbstractIn vitro experiments have shown GRASP65 (GORASP1) and GRASP55 (GORASP2) proteins function in stacking Golgi cisternae. However, in vivo depletion of GORASPs in metazoans have given equivocal results. We have generated a mouse lacking both GORASPs and find that Golgi cisternae remained stacked. However, the stacks are disconnected laterally from each other and the cisternal cross-sectional diameters are significantly reduced compared to their normal counterparts. These data support earlier findings on the role of GORASPs in linking stacks and we suggest that unlinking of stacks affects dynamic control of COPI budding and vesicle fusion at the rims. The net result is that cisternal cores remain stacked, but cisternal diameter is reduced by rim consumption.


2009 ◽  
Vol 187 (2) ◽  
pp. 295-310 ◽  
Author(s):  
Cynthia F. Barber ◽  
Ramon A. Jorquera ◽  
Jan E. Melom ◽  
J. Troy Littleton

Ca2+ influx into synaptic compartments during activity is a key mediator of neuronal plasticity. Although the role of presynaptic Ca2+ in triggering vesicle fusion though the Ca2+ sensor synaptotagmin 1 (Syt 1) is established, molecular mechanisms that underlie responses to postsynaptic Ca2+ influx remain unclear. In this study, we demonstrate that fusion-competent Syt 4 vesicles localize postsynaptically at both neuromuscular junctions (NMJs) and central nervous system synapses in Drosophila melanogaster. Syt 4 messenger RNA and protein expression are strongly regulated by neuronal activity, whereas altered levels of postsynaptic Syt 4 modify synaptic growth and presynaptic release properties. Syt 4 is required for known forms of activity-dependent structural plasticity at NMJs. Synaptic proliferation and retrograde signaling mediated by Syt 4 requires functional C2A and C2B Ca2+–binding sites, as well as serine 284, an evolutionarily conserved substitution for a key Ca2+-binding aspartic acid found in other synaptotagmins. These data suggest that Syt 4 regulates activity-dependent release of postsynaptic retrograde signals that promote synaptic plasticity, similar to the role of Syt 1 as a Ca2+ sensor for presynaptic vesicle fusion.


2015 ◽  
Vol 137 (40) ◽  
pp. 12873-12883 ◽  
Author(s):  
Haijia Yu ◽  
Shailendra S. Rathore ◽  
Chong Shen ◽  
Yinghui Liu ◽  
Yan Ouyang ◽  
...  

2012 ◽  
Vol 17 (7) ◽  
pp. 993-998 ◽  
Author(s):  
Kris F. Sachsenmeier ◽  
Carl Hay ◽  
Erin Brand ◽  
Lori Clarke ◽  
Kim Rosenthal ◽  
...  

5′-Ectonucleotidase (NT5E) catalyzes the conversion of adenosine monophosphate to adenosine and free phosphate. The role of this ectonucleotidase and its production of adenosine are linked with immune function, angiogenesis, and cancer. NT5E activity is typically assayed either by chromatographic quantification of substrates and products using high-performance liquid chromatography (HPLC) or by quantification of free phosphate using malachite green. These methods are not suitable for robust screening assays of NT5E activity. HPLC is not readily suitable for the rapid and efficient assay of multiple samples and malachite green is highly sensitive to the phosphate-containing buffers common in various media and sample buffers. Here the development and validation of a novel high-throughput ectonucleotidase screening assay are described, which makes use of a luciferase-based assay reagent, the Promega CellTiter-Glo kit, to measure the catabolism of AMP by NT5E. This multiwell plate-based assay facilitates the screening of potential ectonucleotidase antagonists and is unaffected by the presence of contaminating phosphate molecules present in screening samples.


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