Publications by authors named "Charlotte F Kelley"
Article Synopsis
- Focal adhesions are assemblies formed around activated integrin receptors, and the study investigates how these structures maintain their flexible, liquid-like properties in the cell.
- Researchers reconstitute focal adhesion components, observing that proteins like talin and vinculin undergo liquid-liquid phase separation, particularly when interacting with specific membrane lipids.
- The findings suggest that lipid binding activates these proteins, leading to their clustering on membranes, which helps early focal adhesions stay organized yet dynamic, allowing for quick assembly and disassembly.
Article Synopsis
- The study focuses on how actin assembly, necessary for processes like endocytosis at synaptic membranes, is tightly controlled by specific proteins to ensure effective membrane remodeling.
- It explains that the endocytic proteins Nwk/FCHSD2, Dap160/intersectin, and WASp interact in a way that both relieves autoinhibition and encourages targeted actin assembly during synaptic activity.
- Ultimately, the research highlights that these protein interactions not only prevent unwanted actin structures but also enhance synaptic endocytosis, indicating a dual role in regulating actin assembly in neurons.
Article Synopsis
- The development of minimal cell division machineries in synthetic biology focuses on controlling large structures like Giant Unilamellar Vesicles (GUVs) using active elements much larger than molecular structures.
- The study employs advanced methods to encapsulate and analyze bundled actin filaments in GUVs, revealing key parameters that allow actin polymerization to mimic various cellular networks.
- Findings indicate that effective membrane binding is essential for forming stable actin rings, which contract and deform the vesicles when activated by myosin motors, while cortex-like actin networks can stabilize these deformations.
Focal adhesions (FA) are large macromolecular assemblies which help transmit mechanical forces and regulatory signals between the extracellular matrix and an interacting cell. Two key proteins talin and vinculin connecting integrin to actomyosin networks in the cell. Both proteins bind to F-actin and each other, providing a foundation for network formation within FAs.
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- Focal adhesions (FAs) are important for cell functions like adhesion and movement, with talin being a key protein that links integrins to the cytoskeleton.
- Researchers used cryoelectron microscopy to explore the structure of talin1, finding it has a self-inhibiting mechanism that prevents integrin activation when needed.
- The study shows that talin can switch between a compact form and a longer, active conformation, which is essential for regulating cell adhesion and signaling processes.
Article Synopsis
- Autoinhibitory interactions between the SH3 and F-BAR domains of F-BAR proteins regulate membrane remodeling, but the structural basis of this autoregulation and its effect on cellular interactions are not well understood.
- The study utilized single-particle electron microscopy to analyze the F-BAR protein Nervous Wreck (Nwk) in soluble and membrane-bound forms, revealing that the SH3 domains reposition rather than fully detach upon membrane binding.
- Findings indicate that Nwk's autoregulation limits the activity of SH3 domains in actin filament assembly and affects synaptic growth and organization in Drosophila neurons, suggesting a coordinated relationship between membrane interactions and SH3 domain functions.
Article Synopsis
- F-BAR domain proteins are crucial for sensing and shaping membrane curvature by interacting with specific negatively charged lipids but how these interactions are controlled is not well understood.
- * In this study, researchers found that the Drosophila Nervous Wreck (Nwk) protein uses a C-terminal SH3 domain to autoregulate its own F-BAR domain, impacting how it interacts with membranes.
- * Autoregulation does not simply act as a switch; instead, it enhances Nwk's ability to form higher-order structures and affects membrane deformation, depending on the negative charge of the membrane composition.*
F-BAR domains form crescent-shaped dimers that bind to and deform lipid bilayers, and play a role in many cellular processes requiring membrane remodeling, including endocytosis and cell morphogenesis. Nervous Wreck (NWK) encodes an F-BAR/SH3 protein that regulates synapse growth in Drosophila. Unlike conventional F-BAR proteins that assemble tip-to-tip into filaments and helical arrays around membrane tubules, the Nwk F-BAR domain instead assembles into zigzags, creating ridges and periodic scallops on membranes in vitro.
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- Eukaryotic cells rely on F-BAR domain proteins, which are capable of bending membranes for shaping cellular compartments, but their varying membrane-deforming activities are not fully understood.
- The Nwk protein's F-BAR domain forms a unique zigzag structure that enhances its ability to create distinct membrane shapes, differing from other F-BAR proteins.
- This study reveals how structural features of the Nwk F-BAR domain contribute to its membrane sculpting abilities, highlighting a new aspect of how F-BAR proteins can induce various membrane curvatures.