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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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Strong contact points between adjacent cells anchor them to each other, forming tissues. Such anchoring junctions are of two types –  adherens junctions and desmosomes. Adherens junctions are abundant in tissues such as  epithelium and endothelium, forming a continuous zone of adhesion called the adhesion belt. In other tissues, such as  heart muscle, they appear as clusters, linking the cells to produce coordinated heart muscle contraction.
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ANKS4B Is Essential for Intermicrovillar Adhesion Complex Formation.

Scott W Crawley1, Meredith L Weck1, Nathan E Grega-Larson1

  • 1Department of Cell and Developmental Biology, Vanderbilt University School of Medicine, 3154 MRB III, PMB 407935, 465 21(st) Avenue South, Nashville, TN 37240-7935, USA.

Developmental Cell
|January 27, 2016
PubMed
Summary
This summary is machine-generated.

Ankyrin repeat and sterile alpha motif domain containing 4B (ANKS4B) is crucial for brush border assembly and intermicrovillar adhesion. It forms a complex with USH1C and MYO7B, revealing a hierarchy in molecular interactions essential for cell structure.

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Apical specializations in epithelial cells rely on protocadherin-based adhesion.
  • The cytoplasmic complex regulating protocadherin in the enterocyte brush border is not fully understood.

Purpose of the Study:

  • To investigate the role of ANKS4B in brush border assembly and intermicrovillar adhesion.
  • To elucidate the molecular interactions and assembly logic of the protocadherin-associated complex.

Main Methods:

  • Immunofluorescence microscopy to determine ANKS4B localization.
  • Co-immunoprecipitation assays to identify protein interactions.
  • Functional assays to assess ANKS4B's role in adhesion.

Main Results:

  • ANKS4B localizes to microvilli tips and is essential for intermicrovillar adhesion.
  • ANKS4B interacts with USH1C and MYO7B, linking protocadherins to the actin cytoskeleton.
  • A tripartite complex of ANKS4B, USH1C, and MYO7B requires USH1C-mediated activation of ANKS4B and MYO7B.

Conclusions:

  • ANKS4B plays a vital role in brush border assembly and intermicrovillar adhesion.
  • A hierarchical assembly mechanism involving USH1C activation is critical for complex formation.
  • Findings provide insights into Usher syndrome and related diseases caused by mutations in USH1C and ankyrin repeat proteins.