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Related Concept Videos

Intracellular Signaling Affects Focal Adhesions01:17

Intracellular Signaling Affects Focal Adhesions

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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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Integrins bind ligands and transmit information from outside the cell to inside or vice-versa through an "outside-in signaling" or "inside-out signaling."
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Animal and protozoan cells do not have cell walls to help maintain shape and provide structural stability. Instead, these eukaryotic cells secrete a sticky mass of carbohydrates and proteins into the spaces between adjacent cells. This network of proteins and molecules is called an extracellular matrix or ECM.
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Phosphoinositides are a group of phospholipids containing a glycerol backbone with two fatty acid chains and a phosphate attached to a myoinositol sugar ring. The inositol head group extends into the cytoplasm, where it is modified by adding phosphate groups to form phosphatidylinositol phosphates or PIPs.
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Tension Response at Adherens Junctions01:26

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The adherens junctions that anchor cells together are multi-protein complexes that dynamically adapt to mechanical stimuli such as tensile forces and shear stress. Mechanosensory proteins in these junctions can sense such mechanical stimuli and undergo a shift in their conformation, resulting in an altered function — a process called mechanotransduction.
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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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YAP phosphorylation within integrin adhesions: Insights from a computational model.

Hamidreza Jafarinia1, Lidan Shi2, Haguy Wolfenson2

  • 1MERLN Institute for Technology-Inspired Regenerative Medicine, Department of Cell Biology-Inspired Tissue Engineering, Maastricht University, Maastricht, the Netherlands.

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Yes-associated protein (YAP) phosphorylation, crucial for cell response, is influenced by adhesion size and dynamics. Our model shows smaller adhesions and higher diffusion increase phosphorylated YAP (pYAP), impacting apoptosis.

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Area of Science:

  • Cell Biology
  • Biophysics
  • Mechanobiology

Background:

  • Yes-associated protein (YAP) mediates cellular responses to mechanical and biochemical cues.
  • YAP plays a role in apoptosis, with phosphorylation at Y357 linked to nuclear translocation and cell death on soft substrates.
  • YAP Y357 phosphorylation is reduced on stiff matrices within larger focal adhesions.

Purpose of the Study:

  • To investigate the dynamics of YAP phosphorylation within integrin adhesions using a stochastic model.
  • To explore how adhesion size, diffusion rates, and binding kinetics influence YAP phosphorylation.
  • To elucidate the interplay of adhesion lifetime and dephosphorylation rates on pYAP levels.

Main Methods:

  • Development of a stochastic model to simulate YAP phosphorylation dynamics.
  • Analysis of the effects of cytosolic diffusion rate on phosphorylated YAP (pYAP) levels.
  • Investigation of the impact of binding site availability and distribution on pYAP.

Main Results:

  • Increased cytosolic diffusion rate of YAP correlates with elevated pYAP levels.
  • Smaller adhesions (more binding sites) increase pYAP, especially at lower diffusion rates.
  • Adhesion lifetime, binding/release rates, and dephosphorylation rates significantly modulate adhesion-size-dependent YAP phosphorylation.

Conclusions:

  • Adhesion size and dynamics are critical factors in regulating YAP phosphorylation.
  • The model provides insights into the mechanotransduction of YAP.
  • Findings offer a basis for experimental validation of YAP phosphorylation regulation in cellular processes.