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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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In the renin-angiotensin-aldosterone system, a hormone called angiotensin II plays a crucial role. It binds to the AT1 receptors in vascular smooth muscles coupled with Gq proteins. The activation of these receptors activates an enzyme called phospholipase C, which releases two molecules: inositol trisphosphate and diacylglycerol. These molecules cause a chain reaction that leads to the phosphorylation of myosin light chains and promotes interaction between actin and myosin, leading to smooth...
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In animal cells, the extracellular matrix allows cells within tissues to withstand external stresses and transmits signals from the outside of the cell to the inside. The extracellular matrix is extensive, and its composition varies between different types of tissues. For example, the reticular fibers and ground substance make up the ECM in loose connective tissue, while collagen and bone minerals make up the ECM of bone tissue. 
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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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Structural Rearrangement of the AT1 Receptor Modulated by Membrane Thickness and Tension.

Bharat Poudel1, Juan M Vanegas1

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Membrane thickness and tension significantly influence the activation of the angiotensin II type 1 (AT1) receptor, a key protein in cardiovascular regulation. These mechanical factors stabilize receptor states and drive structural changes, impacting signaling pathways.

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Area of Science:

  • Biophysics
  • Molecular Biology
  • Cardiovascular Physiology

Background:

  • Mechanosensitive (MS) proteins, including G-protein coupled receptors (GPCRs), transduce mechanical stimuli into cellular signals.
  • The angiotensin II type 1 (AT1) receptor is crucial for cardiovascular regulation and implicated in hypertension and heart failure.
  • Understanding membrane-mediated AT1 receptor activation is vital, particularly concerning biased agonism.

Purpose of the Study:

  • To investigate the impact of the local membrane environment on AT1 receptor activation using molecular dynamics (MD) simulations.
  • To elucidate the role of membrane properties like thickness and tension in AT1 receptor conformational dynamics and signaling.

Main Methods:

  • Extensive molecular dynamics (MD) simulations were employed to model the AT1 receptor within varying membrane environments.
  • Analysis focused on receptor state stability, dynamic transitions, and structural changes induced by membrane properties.

Main Results:

  • Membrane thickness was found to significantly affect the stability of both active and inactive AT1 receptor states and their interconversion.
  • Increased membrane tension promoted large structural rearrangements in the inactive AT1 receptor, including outward movement of transmembrane helix 6.
  • These tension-induced changes stabilize intermediate conformations that resemble active states.

Conclusions:

  • The local membrane environment, specifically thickness and tension, plays a critical role in modulating AT1 receptor activation dynamics.
  • Simulation findings provide a framework for understanding how membrane-mediated stimuli facilitate AT1 receptor activation via the β-arrestin pathway.
  • Comparison with AlphaFold 2 predictions offers insights into the structural basis of mechanosensitive GPCR activation.