Publications by authors named "Emily M Messelaar"
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
- 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.*
Membranes form elaborate structures that are highly tailored to their specialized cellular functions, yet the mechanisms by which these structures are shaped remain poorly understood. Here, we show that the conserved membrane-remodeling C-terminal Eps15 Homology Domain (EHD) protein Past1 is required for the normal assembly of the subsynaptic muscle membrane reticulum (SSR) at the Drosophila melanogaster larval neuromuscular junction (NMJ). past1 mutants exhibit altered NMJ morphology, decreased synaptic transmission, reduced glutamate receptor levels, and a deficit in synaptic homeostasis.
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