Single molecule tracking and super-resolution microscopy of integrin adhesion proteins and actin in developing Drosophila muscle attachment sites reveals that nanotopography triggered by Arp2/3-dependent actin protrusions promotes stable adhesion formation. The nanodomains formed during this process confine the diffusion of integrins and promote their immobilization. Spatial confinement is also applied to the motion of actin filaments, resulting in enhanced mechanical connection with the integrin adhesion complex. Fabricated nano-structured surfaces mimicking the nanotopography observed in living tissue are able to recapitulate the formation of these adhesions in isolated muscle cells and the confinement of integrin diffusion. These results emphasize the importance of geometrical regulation of tissue morphogenesis at a single molecule level.
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http://dx.doi.org/10.1002/cm.21970 | DOI Listing |
Cytoskeleton (Hoboken)
January 2025
Interdisciplinary Institute for Neuroscience, Université Bordeaux, CNRS, Bordeaux, France.
Single molecule tracking and super-resolution microscopy of integrin adhesion proteins and actin in developing Drosophila muscle attachment sites reveals that nanotopography triggered by Arp2/3-dependent actin protrusions promotes stable adhesion formation. The nanodomains formed during this process confine the diffusion of integrins and promote their immobilization. Spatial confinement is also applied to the motion of actin filaments, resulting in enhanced mechanical connection with the integrin adhesion complex.
View Article and Find Full Text PDFProc Natl Acad Sci U S A
January 2025
Department of Cell & Molecular Biology, Uppsala University, Uppsala SE-75124, Sweden.
The bacterial chaperone Trigger factor (TF) binds to ribosome-nascent chain complexes (RNCs) and cotranslationally aids the folding of proteins in bacteria. Decades of studies have given a broad, but often conflicting, description of the substrate specificity of TF, its RNC-binding dynamics, and competition with other RNC-binding factors, such as the Signal Recognition Particle (SRP). Previous RNC-binding kinetics experiments were commonly conducted on stalled RNCs in reconstituted systems, and consequently, may not be representative of the interaction of TF with ribosomes translating mRNA in the cytoplasm of the cell.
View Article and Find Full Text PDFJACS Au
December 2024
Department of Chemistry and HKU-CAS Joint Laboratory of Metallomics for Health and Environment, The University of Hong Kong, Pokfulam Road, Hong Kong, SAR, P.R. China.
Metal ions, either essential or therapeutic, play critical roles in life processes or in the treatment of diseases. Proteins and enzymes are involved in metal homeostasis and the action of metallodrugs. Imaging and identifying these metal-binding proteins will facilitate the elucidation of metal-mediated life processes.
View Article and Find Full Text PDFEBioMedicine
December 2024
Physics for Medicine Paris, INSERM U1273, ESPCI Paris, CNRS UMR 8063, PSL Research University, Paris, France.
Background: Neovascularisation of carotid plaques contributes to their vulnerability. Current imaging methods such as contrast-enhanced ultrasound (CEUS) usually lack the required spatial resolution and quantification capability for precise neovessels identification. We aimed at quantifying plaque vascularisation with ultrasound localization microscopy (ULM) and compared the results to histological analysis.
View Article and Find Full Text PDFAdv Sci (Weinh)
December 2024
Department of Bioengineering, Department of Electrical and Computer Engineering, Beckman Institute for Advanced Science and Technology, Cancer Center at Illinois, University of Illinois Urbana-Champaign, Urbana, IL, 61801, USA.
High-resolution optical microscopy, particularly super-resolution localization microscopy, requires precise real-time drift correction to maintain constant focus at nanoscale precision during the prolonged data acquisition. Existing methods, such as fiducial marker tracking, reflection monitoring, and bright-field image correlation, each provide certain advantages but are limited in their broad applicability. In this work, a versatile and robust drift correction technique is presented for single-molecule localization-based super-resolution microscopy.
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