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Cryo-EM structures of cardiac muscle α-actin mutants M305L and A331P give insights into the structural mechanisms of hypertrophic cardiomyopathy.
Eur J Cell Biol
December 2024
Department of Physiology and Cell Biology, Dorothy M. Davis Heart and Lung Research Institute, College of Medicine, The Ohio State University, Columbus, OH, USA. Electronic address:
Cardiac muscle α-actin is a key protein of the thin filament in the muscle sarcomere that, together with myosin thick filaments, produce force and contraction important for normal heart function. Missense mutations in cardiac muscle α-actin can cause hypertrophic cardiomyopathy, a complex disorder of the heart characterized by hypercontractility at the molecular scale that leads to diverse clinical phenotypes. While the clinical aspects of hypertrophic cardiomyopathy have been extensively studied, the molecular mechanisms of missense mutations in cardiac muscle α-actin that cause the disease remain largely elusive.
View Article and Find Full Text PDFCoupling of Spectrin Repeat Modules for the Assembly of Nanorods and Presentation of Protein Domains.
ACS Nano
October 2024
Department of Synthetic Biology and Immunology, National Institute of Chemistry, SI-1000 Ljubljana, Slovenia.
Article Synopsis
- Modular protein engineering allows for the creation of high-molecular-weight assemblies and nanoscale biomaterials with precision, inspired by the structure of human dystrophin.
- The study focuses on designing elongated nanorods using a module of three tandem spectrin repeats that self-assemble through coiled-coil peptides, ensuring structural integrity and continuity of the α-helix.
- The resulting rigid rods, measured by advanced microscopy techniques, can be equipped with various proteins or peptides along their length, showcasing their potential as functionalized biomaterials in research and applications.
Myosin II tension sensors visualize force generation within the actin cytoskeleton in living cells.
J Cell Sci
October 2024
Enabling Technologies Group, Sanford Research, Sioux Falls, SD 57104, USA.
Article Synopsis
- Nonmuscle myosin II (NMII) is crucial for various cellular activities, including cell division and muscle contraction, but measuring the forces it generates in live cells has been challenging.
- A new FRET-based tension sensor has been developed to directly measure the forces associated with NMII along the actin network, using advanced imaging techniques like FLIM-FRET.
- The findings reveal that the forces produced by NMII isoform B (NMIIB) can vary significantly in different locations and times within the cell, suggesting this sensor could help understand the dynamics of cytoskeletal contractility in various cellular processes.
Actomyosin contraction in the follicular epithelium provides the major mechanical force for follicle rupture during ovulation.
Proc Natl Acad Sci U S A
September 2024
Department of Physiology and Neurobiology, University of Connecticut, Storrs, CT 06269.
Ovulation is critical for sexual reproduction and consists of the process of liberating fertilizable oocytes from their somatic follicle capsules, also known as follicle rupture. The mechanical force for oocyte expulsion is largely unknown in many species. Our previous work demonstrated that ovulation, as in mammals, requires the proteolytic degradation of the posterior follicle wall and follicle rupture to release the mature oocyte from a layer of somatic follicle cells.
View Article and Find Full Text PDFAn actomyosin network organizes niche morphology and responds to feedback from recruited stem cells.
Curr Biol
September 2024
Department of Cell and Developmental Biology, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA 19104, USA; Institute for Regenerative Medicine, University of Pennsylvania, Philadelphia, PA 19104, USA. Electronic address:
Stem cells often rely on signals from a niche, which in many tissues adopts a precise morphology. What remains elusive is how niches are formed and how morphology impacts function. To address this, we leverage the Drosophila gonadal niche, which affords genetic tractability and live-imaging.
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