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The important interplay between metal ions and the intermediate filament protein vimentin.
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Department of Chemistry, University of California, Davis, CA, USA.
Vimentin is a principal intermediate filament (IF) protein that is essential for maintaining cytoskeleton architecture and cellular mechanical integrity. Growing evidence is revealing that metal ions play critical roles in modulating the structure, assembly, and mechanics of vimentin IFs. Despite this, a detailed molecular-level understanding of vimentin-metal interactions and its functional consequences remains incomplete.
View Article and Find Full Text PDFComprehensive in silico analyses of keratin heterodimerisation.
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Institute of Molecular Pharmacology, Medical Faculty, RWTH Aachen University, Wendlingweg 2, Aachen 52074, Germany. Electronic address:
Keratins are the largest and most diverse group of intermediate filament proteins, providing structural integrity and mechanical strength to epithelial cells. Although their assembly as heterodimers is well established, the specific pairing preferences and molecular basis of keratin dimerisation remain largely unknown. Here, we employ a high-throughput computational pipeline that integrates AlphaFold Multimer (AFM) modelling, VoroIF-GNN interaction interface quality assessment, interaction energy calculations and structural comparisons with experimentally solved structures to systematically investigate keratin heterodimerisation and to provide a guideline for further analysis of intermediate filament assembly.
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Thyroid lesions associated with DICER1 syndrome include multifocal hyperplastic and benign neoplastic proliferations (follicular nodular disease) with characteristic macrofollicular and/or intrafollicular centripetal papillary growth patterns, frequently associated with atrophic and involutional changes. There are also well-differentiated thyroid carcinomas showing intermediate-type nuclei, sometimes combining high-grade areas (tumor-in-tumor pattern) and poorly differentiated carcinomas. Here, for the first time, we describe an encapsulated follicular cell thyroid tumor showing a mixed follicular and morular growth pattern, which presented in an 11-year-old girl with follicular nodular disease and a constitutional (germline) DICER1 p.
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Cells round up when they enter mitosis and maintain this rounded morphology until they pass the spindle assembly checkpoint during anaphase. However, the mechanisms that regulate and maintain this transient spherical state remain unclear. In this study, we demonstrate that both astral microtubules and Aurora B kinase are required to maintain cortex stability during prometaphase.
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Nat Cell Biol
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Department of Cell and Developmental Biology, Northwestern University Feinberg School of Medicine, Chicago, IL, USA.
Vimentin is a cytoskeletal intermediate filament protein that governs the form and function of mesenchymal cells, although the mechanistic details have been poorly understood. Here we highlight recent findings that reveal the diverse role of vimentin in dynamically organizing intracellular architecture and enhancing mechanical resilience. The exceptional deformability of vimentin can now be understood from its high-resolution three-dimensional structure resolved using cryo-electron microscopy.
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