Publications by authors named "Michelle F Marchan"

Membrane contact sites (MCSs) are sites of close apposition between two organelles used to exchange ions, lipids, and information. Cells respond to changing environmental or developmental conditions by modulating the number, extent, or duration of MCSs. Because of their small size and dynamic nature, tools to study the dynamics of MCSs in live cells have been limited.

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Microtubules are polymers of αβ-tubulin heterodimers that organize into distinct structures in cells. Microtubule-based architectures and networks often contain subsets of microtubule arrays that differ in their dynamic properties. For example, in dividing cells, stable bundles of crosslinked microtubules coexist in close proximity to dynamic non-crosslinked microtubules.

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The dynamic reorganization of microtubule-based cellular structures, such as the spindle and the axoneme, fundamentally depends on the dynamics of individual polymers within multimicrotubule arrays. A major class of enzymes implicated in both the complete demolition and fine size control of microtubule-based arrays are depolymerizing kinesins. How different depolymerases differently remodel microtubule arrays is poorly understood.

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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.
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