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Related Concept Videos

Integrins01:10

Integrins

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.
Some ECM proteins assemble into a basement membrane to which the remaining components adhere. Proteoglycans typically form the bulk of the ECM while fibrous proteins, like collagen,...
Activation of Integrins01:15

Activation of Integrins

Integrins bind ligands and transmit information from outside the cell to inside or vice-versa through an "outside-in signaling" or "inside-out signaling."
In "outside-in signaling," external factors in the extracellular space bind to exposed ligand binding sites on integrins. This causes the inactive protein to undergo a conformational change to become active. Integrins are often clustered on the cell membrane. Repetitive and regularly spaced ligand binding events provide an effective stimulus.
Intracellular Signaling Affects Focal Adhesions01:17

Intracellular Signaling Affects Focal Adhesions

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.
Some...
Selectins01:25

Selectins

Cell adhesion is  an essential aspect of multicellularity. While stable cell interactions usually occur between cells of the same type, transient cell interactions occur between cells of different tissue types, such as between neutrophils and endothelial cells. Selectins are one class of cell adhesion molecules (CAMs) that bind carbohydrate ligands to form transient cell adhesion. They are rod-like proteins with a long extracellular part of variable length ending with the lectin domain, which...
Immunoglobulin-like Cell Adhesion Molecules01:31

Immunoglobulin-like Cell Adhesion Molecules

Immunoglobulin-like cell adhesion molecules or Ig-CAMs are a versatile group of cell surface glycoproteins belonging to the immunoglobulin protein superfamily. Ig-CAMs possess the characteristic immunoglobulin protein domains and other domains such as the fibronectin type III domain. The Ig domains are glycosylated to varying degrees in different Ig-CAMs.
Ig-CAMs exhibit either homophilic binding (to other Ig-CAMs) or heterophilic binding (to other ligands such as integrins). While most Ig-CAMs...
GPI Anchoring of Proteins in the ER Membrane01:29

GPI Anchoring of Proteins in the ER Membrane

GPI-anchoring is a post-translational, reversible protein modification that is ubiquitous in eukaryotes. Such proteins are primarily present on the exoplasmic leaflet of the plasma membrane.
GPI-anchor structure
A sequence of 11 enzymatic reactions results in the synthesis of the complete GPI anchor consisting of a hydrophobic and a hydrophilic portion. The hydrophobic portion comprises phosphatidylinositol, while the hydrophilic part comprises polar groups like phosphoethanolamine,...

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A Flow Cytometry-Based High-Throughput Technique for Screening Integrin-Inhibitory Drugs
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Wech proteins: roles in integrin functions and beyond.

Birgit Löer1, Michael Hoch

  • 1Life & Medical Sciences-Institute, Program Unit Development, Genetics & Molecular Physiology, Laboratory for Molecular Developmental Biology, University of Bonn, Bonn, Germany.

Cell Adhesion & Migration
|March 6, 2009
PubMed
Summary

The newly discovered Drosophila Wech protein is essential for embryonic muscle attachment by linking integrins to the cytoskeleton. This conserved protein is crucial for cell adhesion and tissue development.

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Published on: February 2, 2024

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Area of Science:

  • Cell biology
  • Developmental biology
  • Biochemistry

Background:

  • Integrins are key cell adhesion receptors in animal tissue formation.
  • They link the extracellular matrix to the intracellular cytoskeleton via linker proteins.
  • The Drosophila Wech protein, a conserved RBCC/TRIM family member, is a novel linker complex component.

Purpose of the Study:

  • To identify and characterize the function of the Drosophila Wech protein.
  • To understand Wech's role in embryonic muscle attachment and integrin-mediated adhesion.
  • To investigate the molecular interactions of Wech within the linker complex.

Main Methods:

  • Genetic analysis of wech mutant embryos.
  • Immunolocalization studies to determine Wech protein localization.
  • Biochemical assays to identify Wech-interacting proteins.

Main Results:

  • Wech protein is essential for embryonic muscle attachment in Drosophila.
  • Wech localizes to muscle attachment sites, and its absence causes muscle detachment.
  • Wech localization is dependent on beta-integrin and talin; it interacts with Talin and Integrin-linked kinase (ILK).

Conclusions:

  • Wech is a crucial and evolutionarily conserved regulator of cell-type specific integrin functions.
  • Wech acts as a linker, connecting core components like Talin and ILK.
  • MicroRNA regulation may influence Wech protein activity in integrin-mediated processes.