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Related Concept Videos

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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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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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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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Protein domains are small structurally independent units that are part of a single amino acid chain.  Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
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Transmembrane Domain Oligomerization Propensity determined by ToxR Assay
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Evolution of integrin I domains.

Mark S Johnson1, Bhanupratap Singh Chouhan

  • 1Structural Bioinformatics Laboratory, Biochemistry, Department of Biosciences, Åbo Akademi University, Tykistökatu 6A, 20520, Turku, Finland, johnson4@abo.fi.

Advances in Experimental Medicine and Biology
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The integrin alpha-I (αI) domain, crucial for vertebrate development, emerged in early chordates. Its evolution parallels significant body plan changes in the chordate lineage.

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Area of Science:

  • Evolutionary biology
  • Molecular biology
  • Cell biology

Background:

  • Integrins are cell surface receptors involved in cell adhesion and signaling.
  • The alpha-I (αI) domain, a von Willebrand factor A domain (vWFA), is present in 9 of 18 human integrin alpha subunits.
  • While beta I (βI) domains are ancient, alpha I (αI) domains appeared later in evolutionary history.

Purpose of the Study:

  • To investigate the evolutionary origin and timeline of the integrin alpha I (αI) domain.
  • To understand the relationship between the emergence of αI domains and vertebrate evolution.

Main Methods:

  • Comparative analysis of integrin subunit structures across different species.
  • Phylogenetic reconstruction to trace the evolutionary history of αI domains.

Main Results:

  • The αI domain is found in tunicates and later diverging species, indicating its relatively late evolutionary appearance.
  • Tunicate αI domains differ from human collagen and leukocyte-binding αI domains.
  • Evidence suggests human-type αI domains originated in an ancestor of the earliest vertebrates.

Conclusions:

  • The evolutionary trajectory of integrin αI domains is linked to the significant developmental changes observed in the chordate lineage starting over 550 million years ago.
  • The emergence of αI domains represents a key event in the evolution of vertebrates.