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141 results for “Microtubules”
Motor usage imprints microtubule stability on the shaft - Western blots
<p>Original western blot images that have been used in Andreu-Carbo et al, Motor usage imprints microtubule stability on the shaft, bioRxiv, 10.1101/2021.04.09.439170. For details see the paper.</p>
Interplay of self-organization of microtubule asters and crosslinking protein condensates Data
<p>Data sets from all figures and supplemental figures for manuscript entitled "Interplay of self-organization of microtubule asters and crosslinking protein condensates" accepted at PNAS Nexus.</p>
Suppression of Bend Instability in Microtubule-fd Virus Composite Active Nematics by External Magnetic Field
<p>The shear flow-aligned active nematic within a cuboidal channel is subjected to an external magnetic field (1.8T) in the aligned nematic direction. In the absence of the magnetic field, bend deformations proliferate, generating flows perpendicular to the initial alignment, as seen in the control case where no external field is applied (PIV vectors overlaid on the image for visual representation). Under the influence of the magnetic field, the bend instabilities are quelled, as there are no flows perpendicular to the applied field. Tracer beads are utilized for brightfield imaging in the magnetic field apparatus to distinguish between the conditions, while fluorescently labeled microtubules are observed in the control scenario.</p>
Microtubule retrograde flow retains neuronal polarization in a fluctuating state
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Microtubules growing and shortening under constant force
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Data from: Kif1a and intact microtubules maintain synaptic-vesicle populations at ribbon synapses in zebrafish hair cells
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Paired microtubules growing with a shared load
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Sulfo-SMCC Prevents Annealing of Taxol-Stabilized Microtubules In Vitro
<p>The data consists of raw images analyzed for the paper 'Sulfo-SMCC Prevents Annealing of Taxol-Stabilized Microtubules In Vitro'.</p> <ol> <li>For all files: different data sets are indicated by using prefix A, 2A , 3A for untreated microtubules, and prefix B, 2B, 3B for sulfo-SMCC treated microtubules.</li> <li>Filenames that include time points of 0 h, 6 h, or 24 h show images of treated and untreated microtubules at different time points. This data was used for Fig 1 in the paper.</li> <li>The files with prefix 'dual' refer to data from dual colored experiments. Microtubules were labeled with green dye (488 in filenames) and red dye (TMR in filenames). This data was used for Fig 2 in the paper.</li> <li>The files with prefix 'chemical' are from one experiment with different chemical treatments on MTs. This data was used for Fig 3 in the paper.</li> </ol>
Mechanical stimulation prevents impairment of axon growth and overcompensates microtubules destabilization in cellular models of Alzheimer's disease related Tau pathology
<p>Data and metadata associated to a publication 10.3389/fmed.2025.1519628</p>
Data from: Mechanical fatigue in microtubules
<p><span>Mechanical failure of biological nanostructures due to sustained force application has been studied in great detail. In contrast, fatigue failure arising from repeated application of subcritical stresses has received little attention despite its prominent role in engineering and potentially biology. Here, taxol-stabilized microtubules are up to 256 times bent into sinusoidal shapes of varying wavelength and the frequency of breaking events are observed. These experiments allow the calculation of fatigue life parameters for microtubules. Repeated buckling due to 12.5% compression – equal to the compression level experienced by microtubules in contracting cardiomyocytes – results in failure after in average 5 million cycles, whereas at 20% compression failure occurs after in average one thousand cycles. The fatigue strength (Basquin) exponent B is estimated as -0.06. </span></p>
Non-centrosomal microtubules at kinetochores promote rapid chromosome biorientation during mitosis in human cells
<p>Kinetochore tracking data associated with "Non-centrosomal microtubules at kinetochores promote rapid chromosome biorientation during mitosis in human cells" by Renda, Miles, et al., Current Biology, 2022.</p> <p>Contact Alexey Khodjakov at alexey.khodjakov@health.ny.gov for any questions or processing routines.</p> <p>Each file contains coordinates of centrioles and kinetochores in a single cell. </p> <p>Key to variables:</p> <p>ao -- time point corresponding to anaphase onset</p> <p>cell_id -- comprises three parts: cell type_treatment_number (NaN when only first 15 min of prometaphase were tracked).</p> <p>centrioles -- coordinates of centrioles. Two pages correspond to the two centrosomes, first three columns are X-Y-Z of the mother and the second three columns are X-Y-Z of the daughter centrioles</p> <p>kinetochores -- coordinates of kinetochores. Each page corresponds to a chromosome. X-Y-Z coordinates of sister kinetochores are in columns 1-3 and 4-6.</p> <p>neb -- time point corresponding to nuclear envelope breakdown.</p> <p>total_chrs -- number of chromosomes in the cell</p> <p>tracked -- number of tracks obtained in the cell</p>
Supplemental Data for "Plus and minus ends of microtubule respond asymmetrically to kinesin binding by a long range directionally driven allosteric mechanism"
<p>This is raw data set associated with all the figures in the article "Plus and minus ends of microtubule respond asymmetrically to kinesin binding by a long range directionally driven allosteric mechanism" published in Science Advances by Huong T Vu, Zhechun Zhang, Riina Tehver and D. Thirumalai. </p>
Live-cell imaging of LLC-PK1 cells microtubule dynamics
<p>Stable LLC-PK1 cell line (ATCC:CL-101) was generated and provided by Michael W. Davidson [1,2]. Using a Zeiss Celldiscoverer 7 microscope with a 100X/1.47 NA oil-immersion objective (Plan-Apochromat, Zeiss) and a sCMOS sensor (Hamamatsu, ORCA-Fusion, C15440-20UP), cultured LLC-PK1 cells expressing mEmerald-EB3 were imaged with a 43 nm pixel size. Exposure time was 100 ms, with each frame being captured every two seconds. During acquisition, temperature and CO2 control was set to 37°C and 5%, respectively. mEmerald-EB3 was excited using a 488 nm laser at 1% power, with a FITC filter for fluorescence collection. Acquisition software ZEN 3.2 (blue edition) was used for the imaging protocol.</p> <p>1. Rizzo, M. A., Davidson, M. W., & Piston, D. W. (2009). Fluorescent protein tracking and detection: fluorescent protein structure and color variants. Cold Spring Harbor Protocols, 2009(12), pdb-top63.</p> <p>2. Huang, F., Hartwich, T., Rivera-Molina, F. et al. Video-rate nanoscopy using sCMOS camera–specific single-molecule localization algorithms. Nat Methods 10, 653–658 (2013).</p>
Vimentin supports cell polarization by enhancing centrosome function and microtubule acetylation
<p>Cell polarity is important for controlling cell shape, motility, and cell division processes. Vimentin intermediate filaments are important for cell migration and cell polarization in mesenchymal cells and assembly of vimentin and microtubule networks is dynamically coordinated, but the precise details of how vimentin mediates cell polarity remain unclear. Here, we characterize the effects of vimentin on the structure and function of the centrosome and the stability of microtubule filaments in wild-type and vimentin-null mouse embryonic fibroblasts (mEFs). We find that vimentin mediates the structure of the pericentrosomal material, promotes centrosome-mediated microtubule regrowth, and increases the level of stable acetylated microtubules in the cell. Loss of vimentin also impairs centrosome repositioning during cell polarization and migration processes that occur during wound closure. Our results suggest that vimentin modulates centrosome structure and function as well as microtubule network stability, which has important implications for how cells establish proper cell polarization and persistent migration.</p>
Data associated with the publication "A de novo designed coiled-coil-based switch regulates the microtubule motor kinesin-1"
<p> All raw data required to reproduce the findings in the manuscript ""A de novo designed coiled-coil-based switch regulates the microtubule motor kinesin-1".</p>
The non-mitotic role of HMMR in regulating the localization of TPX2 and the dynamics of microtubules in neurons
<p>A functional nervous system is built upon the proper morphogenesis of neurons to establish the intricate connection between them. The microtubule cytoskeleton is known to play various essential roles in this morphogenetic process. While many microtubule-associated proteins (MAPs) have been demonstrated to participate in neuronal morphogenesis, the function of many more remains to be determined. This study focuses on a MAP called HMMR in mice, which was originally identified as a hyaluronan binding protein and later found to possess microtubule and centrosome binding capacity. HMMR exhibits high abundance on neuronal microtubules and altering the level of HMMR significantly affects the morphology of neurons. Instead of confining to the centrosome(s) like cells in mitosis, HMMR localizes to microtubules along axons and dendrites. Furthermore, transiently expressing HMMR enhances the stability of neuronal microtubules and increases the formation frequency of growing microtubules along the neurites. HMMR regulates the microtubule localization of a non-centrosomal microtubule nucleator TPX2 along the neurite, offering an explanation for how HMMR contributes to the promotion of growing microtubules. This study sheds light on how progenitor cells utilize proteins involved in mitosis for non-mitotic functions.</p>
BioTISR: Microtubules (3D)
<p>3D microtubules data of BioTISR dataset.</p> <p>BioTISR is a biological image dataset for super-resolution microscopy, currently including 2D and 3D time-lapse image pairs of low-and-high resolution images of a variety of biology structures, aiming to provide a high-quality dataset of time-lapse biological SR images for the community to spark more developments of computational SR methods.</p> <p>At present, 2D dataset includes five specimens (clathrin-coated pits, lysosomes, outer mitochondrial membrane, microtubules, and F-actin) acquired with the GI/TIRF-SIM mode and nonlinear SIM mode of our Multi-SIM system, and 3D data includes three specimens (outer mitochondrial membrane, microtubules, and F-actin) acquired with 3D-SIM mode of the Multi-SIM system. For each type of specimen and each imaging modality, we acquired the raw data from at least 50 distinct regions-of-interest (ROI). For each ROI, we acquired two (3D data) or three (2D data) groups of N-phase × M-orientation × T-timepoint raw images with a constant exposure time but increasing the excitation light intensity, where (N, M, T) are (3, 3, 20) for TIRF-SIM and GI-SIM, (5, 5, 10) for nonlinear SIM, and (3, 5, 10) for 3D-SIM.</p> <p>The BioTISR dataset is related to the following paper:<a href="https://doi.org/10.1101/2024.05.04.592503">Chang Qiao, Shuran Liu, Yuwang Wang, Wencong Xu, et al. "Time-lapse Image Super-resolution Neural Network with Reliable Confidence Evaluation for Optical Microscopy." bioRxiv 2024.05.04.592503 (2024)</a>, which is an extension of our previously published <a href="https://doi.org/10.6084/m9.figshare.13264793.v9">BioSR dataset</a> (https://www.nature.com/articles/s41592-020-01048-5).</p>
Tau accelerates tubulin exchange in the microtubule lattice
<p>This dataset contains the data and source code for Figures 1-4 and and the source code for Supplementary Figures S5-S10 from the following publication: </p> <div> <p>Tau accelerates tubulin exchange in the microtubule lattice</p> </div> <div>by</div> <div> </div> <div>Subham Biswas, Rahul Grover, Cordula Reuther, Chetan S. Poojari, M. Reza Shaebani, Mona Grünewald, Amir Zablotsky, Jochen S. Hub, Stefan Diez, Karin John, Laura Schaedel</div> <div> </div> <div>doi: https://doi.org/10.1101/2024.10.05.616777</div>
BioTISR: Microtubules (3D)
<p>3D Microtubules data of BioTISR dataset.</p> <p>BioTISR is a biological image dataset for super-resolution microscopy, currently including 2D and 3D time-lapse image pairs of low-and-high resolution images of a variety of biology structures, aiming to provide a high-quality dataset of time-lapse biological SR images for the community to spark more developments of computational SR methods.</p> <p>At present, 2D dataset includes five specimens (clathrin-coated pits, lysosomes, outer mitochondrial membrane, microtubules, and F-actin) acquired with the GI/TIRF-SIM mode and nonlinear SIM mode of our Multi-SIM system, and 3D data includes three specimens (outer mitochondrial membrane, microtubules, and F-actin) acquired with 3D-SIM mode of the Multi-SIM system. For each type of specimen and each imaging modality, we acquired the raw data from at least 50 distinct regions-of-interest (ROI). For each ROI, we acquired two (3D data) or three (2D data) groups of N-phase × M-orientation × T-timepoint raw images with a constant exposure time but increasing the excitation light intensity, where (N, M, T) are (3, 3, 20) for TIRF-SIM and GI-SIM, (5, 5, 10) for nonlinear SIM, and (3, 5, 10) for 3D-SIM.</p> <p>The BioTISR dataset is related to the following paper:<a href="https://doi.org/10.1101/2024.05.04.592503">Chang Qiao, Shuran Liu, Yuwang Wang, Wencong Xu, et al. "Time-lapse Image Super-resolution Neural Network with Reliable Confidence Evaluation for Optical Microscopy." bioRxiv 2024.05.04.592503 (2024)</a>, which is an extension of our previously published <a href="https://doi.org/10.6084/m9.figshare.13264793.v9">BioSR dataset</a> (https://www.nature.com/articles/s41592-020-01048-5).</p>
Data for: The conserved centrosomin motif, γTuNA, forms a dimer that directly activates microtubule nucleation by the γ-tubulin ring complex (γTuRC)
<p>To establish the microtubule cytoskeleton, the cell must tightly regulate when and where microtubules are nucleated. This regulation involves controlling the initial nucleation template, the γ-tubulin ring complex (γTuRC). Although γTuRC is present throughout the cytoplasm, its activity is restricted to specific sites including the centrosome and Golgi. The well-conserved γ-tubulin nucleation activator (γTuNA) domain has been reported to increase the number of microtubules (MTs) generated by γTuRCs. However, previously we and others observed that γTuNA had a minimal effect on the activity of antibody-purified Xenopus γTuRCs in vitro (Thawani et al., eLife, 2020; Liu et al., 2020). Here we instead report, based on improved versions of γTuRC, γTuNA, and our TIRF assay, the first real-time observation that γTuNA directly increases γTuRC activity in vitro, which is thus a bona fide γTuRC activator. We further validate this effect in Xenopus egg extract. Via mutation analysis, we find that γTuNA is an obligate dimer. Moreover, efficient dimerization as well as γTuNA's L70, F75, and L77 residues are required for binding to and activation of γTuRC. Finally, we find that γTuNA's activating effect opposes inhibitory regulation by stathmin. In sum, our improved assays prove that direct γTuNA binding strongly activates γTuRCs, explaining previously observed effects of γTuNA expression in cells and illuminating how γTuRC-mediated microtubule nucleation is regulated.</p>
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Allen Brain Atlas
Allen Brain Atlas is an Allen Institute collection of brain map atlases, datasets, APIs, and analysis tools covering mouse, human, and non-human primate brain resources.
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DANDI Archive for NWB datasets
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International Brain Laboratory public data
The International Brain Laboratory public data releases expose standardized mouse decision-making experiments, including Neuropixels recordings, widefield calcium imaging, behavior, and session metadata accessed through the ONE API.
OpenNeuro
OpenNeuro is a free, open platform for sharing neuroimaging datasets, with public search, dataset pages, and download paths for web, S3, DataLad, and the OpenNeuro CLI.