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Related Concept Videos

The Contractile Ring02:15

The Contractile Ring

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Contractile rings are composed of microfilaments and are responsible for separating the daughter cells during cytokinesis. Contractile ring assembly proceeds along with other cell cycle events; however, very few mechanistic details are known about the timing and coordination of the contractile rings with the cell cycle.
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Cell polarity is the asymmetric distribution of cellular and membrane components, making one side of the cell different from the other. This polarity is essential to many processes such as embryogenesis, axon migration, glucose transport across epithelial cells, and directional cell migration. A migrating cell responds to intracellular or extracellular signals via molecular cascades that reorganize the actin cytoskeleton to establish this polarity. In these cells, the Rho family proteins Cdc42,...
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Role of Septins01:02

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Septins are the recently discovered fourth major protein component of the cytoskeleton, along with microfilaments, microtubules, and intermediate filaments. These proteins can associate with other cytoskeletal filaments and carry out varied roles or can be free-floating in the cytoplasm.
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Ras and Rho are small monomeric GTPases that act downstream of receptor tyrosine kinase (RTK) and regulate various cellular processes. These GTPases switch between active and inactive states by binding to guanine nucleotides.
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Septins are protein filaments forming the cytoskeleton along with the microtubules, microfilaments, intermediate filaments, and other accessory proteins. In 1971 while studying the cell division cycle in mutant Saccharomyces cerevisiae Harwell et al. first identified the septin-related genes playing a crucial role in yeast cytokinesis. Fluorescence microscopy revealed that these proteins localize at the budding neck as rings. These ring-like proteins were then named Septins by John Pringle, and...
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Rab GTPases act in a regulated cascade during membrane fusion, helping the lipid bilayers mix. The Rab family of proteins are active when bound to GTP, and inactive when bound to GDP. Hence, they act as guanine nucleotide-dependent molecular switches. Rab-GTP recognizes and binds to long or short-range tethering proteins to capture the target vesicle. These tethers coordinate with SNAREs on the vesicle and the target membrane to assemble the trans SNARE complex that locks the mixing bilayers.
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RhoC GTPase Activation Assay
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Local RhoA activation induces anillin-independent septin recruitment in interphase cells.

Shreya Chandrasekar1, Margaret E Utgaard1, Bradley Somerfield1

  • 1Deptartment of Cell and Molecular Physiology, Loyola University Chicago, Stritch School of Medicine, Maywood, IL 60153.

Molecular Biology of the Cell
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Summary

RhoA activation, not myosin changes, drives septin cytoskeleton remodeling. This study clarifies RhoA

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Area of Science:

  • Cell Biology
  • Cytoskeleton Dynamics
  • Molecular Cell Biology

Background:

  • Actin cytoskeleton regulation is crucial for cell shape.
  • RhoA GTPase is known to regulate actomyosin, but its role in septin cytoskeleton control is unclear.
  • Traditional assays struggle to resolve RhoA's spatiotemporal interactions.

Purpose of the Study:

  • To investigate the impact of RhoA and myosin on the septin cytoskeleton.
  • To understand how RhoA signaling influences septin organization.

Main Methods:

  • Utilized optogenetic tools for spatial and temporal control.
  • Manipulated myosin localization and activity.
  • Activated RhoA locally within cells.

Main Results:

  • Local myosin accumulation or increased activity did not alter septin architecture.
  • Local RhoA activation led to a significant increase in septin accumulation.
  • This septin increase was independent of the anillin scaffolding protein.

Conclusions:

  • RhoA signaling directly stimulates septin cytoskeleton remodeling.
  • Septins may play a broader role in mediating RhoA signaling pathways.
  • Findings advance understanding of cytoskeletal regulation and cell structure.