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Contact-dependent Signaling01:19

Contact-dependent Signaling

Contact-dependent signaling, as the name suggests, requires that communicating cells be in direct contact with each other. This is achieved either through receptor-ligand interactions or by specialized cytoplasmic channels that allow the flow of small molecules between cells. In animal cells, channels called gap junctions facilitate contact-dependent signaling in certain tissues, whereas, plasmodesmata perform a similar function in plants.
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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 basis of semaphorin-plexin signalling.

Bert J C Janssen1, Ross A Robinson, Francesc Pérez-Brangulí

  • 1Division of Structural Biology, Wellcome Trust Centre for Human Genetics, University of Oxford, Oxford OX3 7BN, UK.

Nature
|September 30, 2010
PubMed
Summary
This summary is machine-generated.

Semaphorin-plexin cell signalling relies on bivalent 2:2 complexes. This study reveals the structural basis for semaphorin-plexin interactions, clarifying signalling mechanisms in development and disease.

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Area of Science:

  • Molecular Biology
  • Cell Biology
  • Structural Biology

Background:

  • Cell-cell communication via semaphorin ligands and plexin receptors is crucial for tissue homeostasis, morphogenesis, neural development, cancer, and immune responses.
  • SEMA4D and Sema6A are vertebrate semaphorins that signal through plexin-B and plexin-A receptors, respectively.
  • The structural basis for semaphorin-plexin interactions and plexin signalling specificity was previously unknown.

Purpose of the Study:

  • To elucidate the structural mechanisms underlying semaphorin-plexin interactions and signalling.
  • To determine the extracellular specificity and mechanism controlling plexin signalling.

Main Methods:

  • X-ray crystallography was used to determine the structures of semaphorin-plexin complexes and individual components.
  • Biophysical and cellular assays were employed to investigate the functional consequences of these interactions.

Main Results:

  • Crystal structures revealed how semaphorin dimers bind two plexin molecules, forming a bivalent 2:2 complex essential for signalling.
  • Monomeric semaphorin binding to plexin does not trigger signalling, highlighting the importance of avidity.
  • A conserved structural architecture involving the semaphorin-binding domains (seven-bladed β-propeller) mediates common interaction modes, while variations dictate specificity.

Conclusions:

  • Semaphorin-plexin signalling is triggered by semaphorin-stabilized plexin dimerization, potentially followed by clustering.
  • The findings provide a structural framework for understanding semaphorin-plexin interactions and their roles in diverse biological processes.
  • Conserved and variable structural elements explain both the common signalling mechanism and the specificities observed across different semaphorin-plexin pairs.