Myosin-Is colocalize with Arp2/3 complex-nucleated actin networks at sites of membrane protrusion and invagination, but the mechanisms by which myosin-I motor activity coordinates with branched actin assembly to generate force are unknown. We mimicked the interplay of these proteins using the "comet tail" bead motility assay, where branched actin networks are nucleated by Arp2/3 complex on the surface of beads coated with myosin-I and the WCA domain of N-WASP. We observed that myosin-I increased bead movement efficiency by thinning actin networks without affecting growth rates. Remarkably, myosin-I triggered symmetry breaking and comet-tail formation in dense networks resistant to spontaneous fracturing. Even with arrested actin assembly, myosin-I alone could break the network. Computational modeling recapitulated these observations suggesting myosin-I acts as a repulsive force shaping the network's architecture and boosting its force-generating capacity. We propose that myosin-I leverages its power stroke to amplify the forces generated by Arp2/3 complex-nucleated actin networks.
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http://dx.doi.org/10.1101/2024.02.09.579714 | DOI Listing |
Front Parasitol
March 2024
Departamento de Infectómica y Patogénesis Molecular, Centro de Investigación y de Estudios Avanzados del Instituto Politécnico Nacional [CINVESTAV-Instituto Politécnico Nacional (IPN)], Mexico City, Mexico.
The retromer is a highly conserved eukaryotic complex formed by the cargo selective complex (CSC) and the sorting nexin (SNX) dimer subcomplexes. Its function is protein recycling and recovery from the endosomes to conduct the target molecules to the trans-Golgi network or the plasma membrane. The protozoan responsible for human amoebiasis, , exhibits an active membrane movement and voracious phagocytosis, events in which the retromer may be fully involved.
View Article and Find Full Text PDFZhongguo Zhong Yao Za Zhi
December 2024
Institute of Chinese Materia Medica, China Academy of Chinese Medical Sciences Beijing 100700, China.
This study aimed to investigate the potential role of Colquhounia Root Tablets against bone destruction in rheumatoid arthritis(RA) and its molecular mechanism. The study used ultra-performance liquid chromatography-mass spectrometry to analyze the major components of Colquhounia Root Tablets and predicted its candidate target gene set based on the major components. The key targets of RA bone destruction were obtained through GeneCards and the Database of Genetics and Medical Literature(OMIM), protein-protein interaction(PPI) network was constructed, and the key targets were identified by topological analysis.
View Article and Find Full Text PDFDiabetic kidney disease (DKD) progression is often marked by early glomerular endothelial cell (GEC) dysfunction, including alterations in the fenestration size and number linked to impaired glomerular filtration. However, the cellular mechanisms regulating GEC fenestrations remain poorly understood due to limitations in existing models, challenges in imaging small fenestrations , and inconsistencies between and findings. This study used a logic-based protein-protein interaction network model with normalized Hill functions for dynamics to explore how glucose-mediated signaling dysregulation impacts fenestration dynamics in GECs.
View Article and Find Full Text PDFJ Phys Chem B
January 2025
Department of Computer and Information Sciences, Department of Materials Science and Engineering, University of Delaware, Newark, Delaware 19716, United States.
Liquid phase-separating proteins can form condensates that play an important role in spatial and temporal organization of biological cells. The understanding of the mechanisms that lead to the formation of protein condensates and their interactions with other biomolecules may lead to processing routes for soft materials with tailored geometry and function. Fused in sarcoma (FUS) is an example of a nuclear protein that forms stable complexes, and recent studies have highlighted its ability to wet actin filaments and bundle them into networks.
View Article and Find Full Text PDFStructure
January 2025
Molecular Microbiology, School of Biosciences, University of Sheffield, Sheffield S10 2TN, UK. Electronic address:
The core component of the actin cytoskeleton is the globular protein G-actin, which reversibly polymerizes into filaments (F-actin). Budding yeast possesses a single actin that shares 87%-89% sequence identity with vertebrate actin isoforms. Previous structural studies indicate very close overlap of main-chain backbones.
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