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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,...
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,...
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.
Overview of Cell-Matrix Interactions01:24

Overview of Cell-Matrix Interactions

The extracellular matrix or ECM holds cells together to form a tissue and allows the cells within the tissue to communicate. ECM comprises proteins such as fibronectin, collagen, laminin, etc. The most abundant protein in this space is collagen. Collagen fibers are interwoven with carbohydrate-containing protein molecules called proteoglycans. ECM allows cell migration and provides a structural scaffold at cell adhesion that anchors the cell when the extracellular matrix proteins interact with...
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...
Anchoring Junctions01:03

Anchoring Junctions

Anchoring junctions are multiprotein complexes that help cells connect to other cells and the extracellular matrix. Anchoring junctions are present on the lateral and basal surfaces of cells, providing strong and flexible connections. Focal adhesions are often formed due to cell interactions with the ECM substrata, which initiate signal transduction via kinase cascades and other mechanisms. Together, they provide stability and tissue integrity. There are three types of anchoring junctions:...

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Induction of Adhesion-dependent Signals Using Low-intensity Ultrasound
08:51

Induction of Adhesion-dependent Signals Using Low-intensity Ultrasound

Published on: May 8, 2012

Syndecan and integrin interactomes: large complexes in small spaces.

James A Roper1, Rosalind C Williamson, Mark D Bass

  • 1School of Biochemistry, University of Bristol, University Walk, Bristol BS8 1TD, United Kingdom.

Current Opinion in Structural Biology
|July 31, 2012
PubMed
Summary
This summary is machine-generated.

Syndecans and integrins are cell adhesion proteins. This review explores how cells overcome spatial challenges to regulate cell adhesion formation and signaling.

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Last Updated: May 20, 2026

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Area of Science:

  • Cell biology
  • Biochemistry
  • Structural biology

Background:

  • Syndecans are transmembrane proteoglycans crucial for cell adhesion.
  • They cooperate with integrins to regulate cell adhesion dynamics.
  • Heparan sulphate chains on syndecans engage extracellular ligands, while protein cores signal intracellularly.

Purpose of the Study:

  • To review structural rearrangements cells use to overcome spatial limitations in adhesion formation.
  • To compare the interactomes of syndecans and integrins.
  • To understand the composition and regulation of cell adhesions over time.

Main Methods:

  • Literature review and comparative analysis of syndecan and integrin structures and functions.
  • Analysis of spatial paradoxes in syndecan and integrin cooperation.
  • Exploration of cellular mechanisms for overcoming spatial restrictions in adhesion complexes.

Main Results:

  • Syndecans and integrins face spatial challenges due to differing molecular sizes and signaling domains.
  • Cells employ specific structural rearrangements to bridge these spatial gaps.
  • Comparative interactome analysis reveals insights into adhesion composition and temporal regulation.

Conclusions:

  • Understanding the spatial regulation of syndecan-integrin interactions is key to comprehending cell adhesion.
  • Cellular structural adaptations are vital for efficient signaling and adhesion complex formation.
  • This review provides a framework for future research into cell adhesion mechanisms.