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Cell Polarization by Rho Proteins01:21

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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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A migrating cell changes its shape during the cyclic events of attachment and detachment from the substratum and repositions the cell organelles correspondingly. These complex events are orchestrated by the dynamic cytoskeletal network comprising actin filaments, intermediate filaments, and microtubules. Cytoskeletal crosstalk — the direct and indirect communication between the different components — is crucial for this coordination. Direct communication involves various linker...
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Cells migrating in response to external stimuli form lamellipodia, which are thin membrane protrusions supported by a mesh of linked, branched, or unbranched actin filaments. These actin filaments interact with myosin motor proteins, creating the dynamic actomyosin complex within the cytoskeleton. Contractility, or the ability to generate contractile stress, is inherent to the actomyosin complex. It helps cells detect the stiffness of the surrounding ECM and exert contractile force for...
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Integrins act both as extracellular input receivers and as intracellular processing activators. As their name suggests, integrins are entirely integrated into the membrane structure. Their hydrophobic membrane-spanning regions interact with the phospholipid bilayer's hydrophobic region. These membrane receptors provide extracellular attachment sites for effectors like hormones and growth factors. They activate intracellular response cascades when their effectors are bound and active.
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Blebs are a type of membrane protrusion formed by the internal hydrostatic pressure of the cytoplasm. Blebs are observed in several cell types, including fibroblasts, immune cells, and single-celled organisms like the amoeba. The primary function of blebs is cell locomotion and apoptosis, but they are also found during necrosis and cell division. The life cycle of a bleb comprises an initiation phase followed by the expansion and retraction phases.
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Spatio-Temporal Manipulation of Small GTPase Activity at Subcellular Level and on Timescale of Seconds in Living Cells
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Gradients of Rac1 Nanoclusters Support Spatial Patterns of Rac1 Signaling.

Amanda Remorino1, Simon De Beco1, Fanny Cayrac1

  • 1Laboratoire Physico-Chimie, Institut Curie, CNRS UMR168, Paris-Science Lettres, Universite Pierre et Marie Curie-Paris 6, 75005 Paris, France.

Cell Reports
|November 16, 2017
PubMed
Summary
This summary is machine-generated.

Rac1 (Ras-related C3 botulinum toxin substrate 1) forms nanoclusters, organizing into signaling platforms. These platforms are crucial for cell migration and lamellipodia protrusion dynamics.

Keywords:
Rac1cell polaritynanoclustersoptogeneticssignalingsingle molecule

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biophysics

Background:

  • Rac1 is a key regulator of the actin cytoskeleton, controlling cell shape and motility.
  • Active Rac1 forms gradients at the cell front, driving lamellipodia protrusion during migration.
  • The precise spatial organization of Rac1 has remained incompletely understood.

Purpose of the Study:

  • To investigate the supramolecular organization of Rac1 using advanced imaging techniques.
  • To elucidate the molecular mechanisms underlying Rac1 nanocluster formation and localization.
  • To understand how Rac1 nanoclusters contribute to cellular functions like migration.

Main Methods:

  • Single-molecule imaging
  • Super-resolution microscopy
  • Biosensor imaging

Main Results:

  • Rac1 molecules are organized into nanoclusters, each containing 50-100 molecules.
  • Rac1 nanocluster formation is driven by interactions between its polybasic tail and phosphoinositide lipids (PIP2 and PIP3).
  • Rac1 nanoclusters are enriched in protruding cell regions due to interactions with GEFs, GAPs, and other signaling partners.

Conclusions:

  • Subcellular Rac1 activity patterns are supported by signaling nanodomains.
  • These nanodomains exhibit heterogeneous molecular compositions and act as discrete signaling platforms.
  • This supramolecular organization provides a new layer of regulation for Rac1-mediated cellular processes.