Living systems exhibit self-organization, a phenomenon that enables organisms to perform functions essential for life. The interior of living cells is a crowded environment in which the self-assembly of cytoskeletal networks is spatially constrained by membranes and organelles. Cytoskeletal filaments undergo active condensation in the presence of crosslinking motor proteins. In past studies, confinement has been shown to alter the morphology of active condensates. Here, we perform simulations to explore systems of filaments and crosslinking motors in a variety of confining geometries. We simulate spatial confinement imposed by hard spherical, cylindrical, and planar boundaries. These systems exhibit non-equilibrium condensation behavior where crosslinking motors condense a fraction of the overall filament population, leading to coexistence of vapor and condensed states. We find that the confinement lengthscale modifies the dynamics and condensate morphology. With end-pausing crosslinking motors, filaments self-organize into half asters and fully-symmetric asters under spherical confinement, polarity-sorted bilayers and bottle-brush-like states under cylindrical confinement, and flattened asters under planar confinement. The number of crosslinking motors controls the size and shape of condensates, with flattened asters becoming hollow and ring-like for larger motor number. End pausing plays a key role affecting condensate morphology: systems with end-pausing motors evolve into aster-like condensates while those with non-end-pausing crosslinking motor proteins evolve into disordered clusters and polarity-sorted bundles.
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http://dx.doi.org/10.3389/fphy.2022.897255 | DOI Listing |
Pathogens
December 2024
Laboratory of Macromolecular Structure, Department of Molecular Biology and Biochemistry, University of California Irvine, Steinhaus Hall, Irvine, CA 92697-3900, USA.
Concatemeric viral DNA is packaged into bacteriophage P22 procapsids via a headful packaging mechanism mediated by a molecular machine consisting of small (gp3) and large (gp2) terminase subunits. Although a negative stain reconstruction exists for the terminase holoenzyme, it is not clear how this complex binds the dodecameric portal protein located at a 5-fold mismatch vertex. Herein, we describe new assemblies for the holoenzyme.
View Article and Find Full Text PDFThe 26S proteasome complex is the hub for regulated protein degradation in the cell. It is composed of two biochemically distinct complexes: the 20S core particle with proteolytic active sites in an internal chamber and the 19S regulatory particle, consisting of a lid and base subcomplex. The base contains ubiquitin receptors and an AAA+ (ATPases associated with various cellular activities) motor that unfolds substrates prior to degradation.
View Article and Find Full Text PDFMater Today Bio
February 2025
Northern Jiangsu People's Hospital, Yangzhou, Jiangsu, China.
Spinal cord injury (SCI) is a neurological condition that causes significant loss of sensory, motor, and autonomic functions below the level of injury. Current clinical treatment strategies often fail to meet expectations. Hyaluronidase is typically associated with tumor progression and bacterial infections.
View Article and Find Full Text PDFJ Neural Eng
January 2025
Chandra Department of Electrical and Computer Engineering, Cockrell School of Engineering, The University of Texas at Austin, Austin 78712 TX, United States of America.
Non-invasive electroencephalograms (EEG)-based brain-computer interfaces (BCIs) play a crucial role in a diverse range of applications, including motor rehabilitation, assistive and communication technologies, holding potential promise to benefit users across various clinical spectrums. Effective integration of these applications into daily life requires systems that provide stable and reliable BCI control for extended periods. Our prior research introduced the AIRTrode, a self-adhesive (A), injectable (I), and room-temperature (RT) spontaneously-crosslinked hydrogel electrode (AIRTrode).
View Article and Find Full Text PDFBiophys Rev
October 2024
Institute for X-Ray Physics, University of Göttingen, Friedrich-Hund-Platz 1, 37077 Göttingen, Germany.
The cytoskeleton is the major mechanical unit of the cell and is essential for cellular processes such as motility, division, and contraction. It consists of three types of biopolymers-actin filaments, microtubules, and intermediate filaments-along with passive cross-linkers and active motor proteins. This composite biological material determines the enormous viscoelastic adaptability of cells to varying mechanical demands.
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