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Related Concept Videos

Fibril-associated Collagen01:11

Fibril-associated Collagen

Fibril-associated collagens are a type of collagens present in the extracellular matrix with interrupted triple helices or FACIT (Fibril-associated collagens interrupted triple-helices). FACIT help connect and attach the collagen fibrils with each other as well as with other proteins of the extracellular matrix.
For example, the type II collagen fibrils in cartilage have covalently bound type IX fibril-associated collagens at regular intervals. Other types of fibril-associated collagens are...
Multi-pass Transmembrane Proteins and β-barrels01:09

Multi-pass Transmembrane Proteins and β-barrels

In multi-pass transmembrane proteins, the polypeptide chain crosses the membrane more than once. The transmembrane polypeptide chain either forms an α-helix or β-strand structure. α-Helix containing multi-pass transmembrane proteins are ubiquitous, whereas β-strand containing ones are mainly found in gram-negative bacteria, mitochondria, and chloroplasts.
α-Helix containing multi-pass transmembrane proteins
Multi-pass transmembrane proteins such as G-protein-linked receptors (GPCRs) and...
Transducer Mechanism: G Protein–Coupled Receptors01:30

Transducer Mechanism: G Protein–Coupled Receptors

G Protein–Coupled Receptors (GPCRs) are membrane-bound receptors that transiently associate with heterotrimeric G proteins and induce an appropriate response to various stimuli. GPCRs regulate critical physiological pathways and are excellent drug targets for treating diseases such as diabetes, cancer, obesity, depression, or Alzheimer's. Nearly 35% of approved drugs implement their therapeutic effects by selectively interacting with specific GPCRs.
GPCRs are also called heptahelical, 7TM, or...
Types of Receptors: Cell Surface Receptors01:28

Types of Receptors: Cell Surface Receptors

Cell-surface receptors, also known as transmembrane receptors, are cell surface, membrane-anchored (integral) proteins that bind to external ligand molecules. This type of receptor spans the plasma membrane and performs signal transduction, converting an extracellular signal into an intracellular signal. Ligands that interact with cell-surface receptors do not have to enter the cell that they affect. Cell-surface receptors are also called cell-specific proteins or markers because they are...
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...
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,...

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Transmembrane Domain Oligomerization Propensity determined by ToxR Assay
06:45

Transmembrane Domain Oligomerization Propensity determined by ToxR Assay

Published on: May 26, 2011

Transmembrane collagen receptors.

Birgit Leitinger1

  • 1National Heart and Lung Institute, Imperial College London, London SW7 2AZ, United Kingdom. b.leitinger@imperial.ac.uk

Annual Review of Cell and Developmental Biology
|May 17, 2011
PubMed
Summary

Collagen receptors, including integrins and discoidin domain receptors, recognize collagen's triple helix. These receptors control cell functions, development, and disease processes.

Area of Science:

  • Biochemistry
  • Cell Biology
  • Molecular Biology

Background:

  • Collagen is the most abundant animal protein, crucial for extracellular matrix structure and cellular functions like growth and differentiation.
  • Collagens feature triple-helical regions that mediate interactions with various proteins, notably cell surface receptors.
  • Transmembrane receptors such as integrins, discoidin domain receptors, glycoprotein VI, and leukocyte-associated immunoglobulin-like receptor-1 recognize the collagen triple helix.

Purpose of the Study:

  • To discuss collagen receptors, focusing on their molecular mechanisms of collagen recognition.
  • To explore the signaling and developmental roles of these collagen receptors.
  • To examine the involvement of collagen receptors in various disease states.

Main Methods:

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Imaging Denatured Collagen Strands In vivo and Ex vivo via Photo-triggered Hybridization of Caged Collagen Mimetic Peptides
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Imaging Denatured Collagen Strands In vivo and Ex vivo via Photo-triggered Hybridization of Caged Collagen Mimetic Peptides

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Mammalian Cell Division in 3D Matrices via Quantitative Confocal Reflection Microscopy
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Mammalian Cell Division in 3D Matrices via Quantitative Confocal Reflection Microscopy

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Last Updated: Jun 2, 2026

Transmembrane Domain Oligomerization Propensity determined by ToxR Assay
06:45

Transmembrane Domain Oligomerization Propensity determined by ToxR Assay

Published on: May 26, 2011

Imaging Denatured Collagen Strands In vivo and Ex vivo via Photo-triggered Hybridization of Caged Collagen Mimetic Peptides
07:03

Imaging Denatured Collagen Strands In vivo and Ex vivo via Photo-triggered Hybridization of Caged Collagen Mimetic Peptides

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Mammalian Cell Division in 3D Matrices via Quantitative Confocal Reflection Microscopy
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Mammalian Cell Division in 3D Matrices via Quantitative Confocal Reflection Microscopy

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  • Review of scientific literature on collagen structure and function.
  • Analysis of the molecular interactions between collagen and its receptors.
  • Synthesis of data on the signaling pathways regulated by collagen receptors.
  • Examination of the pathological relevance of collagen-receptor interactions.

Main Results:

  • Identified four main classes of transmembrane collagen receptors: integrins, discoidin domain receptors, glycoprotein VI, and leukocyte-associated immunoglobulin-like receptor-1.
  • Detailed the molecular basis for how these receptors recognize the collagen triple helix.
  • Highlighted the diverse cellular functions regulated by collagen receptors, including adhesion, migration, hemostasis, and immune responses.
  • Summarized the roles of these receptors in development and disease pathogenesis.

Conclusions:

  • Collagen receptors are critical mediators of cell-matrix communication, translating collagen structure into cellular responses.
  • Understanding these receptors provides insights into fundamental biological processes and disease mechanisms.
  • Targeting collagen-receptor interactions may offer therapeutic strategies for various conditions.