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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,...
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...
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...
Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
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...

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Polydom/SVEP1 is a ligand for integrin α9β1.

Ryoko Sato-Nishiuchi1, Itsuko Nakano, Akio Ozawa

  • 1Institute for Protein Research, Osaka University, Suita, Osaka 565-0871, Japan.

The Journal of Biological Chemistry
|June 2, 2012
PubMed
Summary

Polydom (SVEP1) is identified as a novel, high-affinity ligand for integrin α9β1. This discovery reveals a key interaction in cell adhesion and identifies a previously unknown physiological ligand in mouse tissues.

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Integrin α9β1 plays a role in cell adhesion, but its physiological ligands with high affinity remain largely unknown.
  • Known ligands like tenascin-C and osteopontin exhibit lower binding affinities compared to other integrin-ligand interactions.

Purpose of the Study:

  • To identify novel physiological ligands for integrin α9β1.
  • To characterize the binding interaction between polydom (SVEP1) and integrin α9β1.

Main Methods:

  • Recombinant protein expression and purification.
  • Integrin binding assays using purified proteins and synthetic peptides.
  • Alanine-scanning mutagenesis to map the binding site.
  • Immunohistochemistry and in situ binding assays on mouse embryonic tissues.

Main Results:

  • Polydom (SVEP1) binds directly to integrin α9β1 with significantly higher affinity than previously known ligands.
  • The integrin-binding site was mapped to the 21st complement control protein domain of polydom, specifically the EDDMMEVPY sequence.
  • Polydom colocalizes with integrin α9 in various mouse embryonic organs and mediates significant integrin α9β1 binding in tissues.

Conclusions:

  • Polydom (SVEP1) is a newly discovered, high-affinity physiological ligand for integrin α9β1.
  • The identified binding site and sequence are crucial for the interaction between polydom and integrin α9β1.
  • This finding advances our understanding of integrin-mediated cell adhesion and identifies a key player in tissue development.