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Related Concept Videos

Fibronectins Connect Cells with ECM01:25

Fibronectins Connect Cells with ECM

Fibronectin is an adhesive glycoprotein present in the extracellular matrix of embryogenic and adult tissue. These molecules primarily aid in regulating cell motility and attachment. A fibronectin molecule is composed of two identical polypeptide chains attached to each other by a pair of disulfide bonds at the C-terminal.
Both proteoglycans and collagen are attached to fibronectin proteins, which, in turn, are attached to integrin proteins. These integrin proteins interact with transmembrane...
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...
Formation of Higher-order Actin Filaments01:11

Formation of Higher-order Actin Filaments

The polymerization of G-actin monomers into filamentous F-actin is a multi-step process. Once the F-actins are formed, they can bundle together in different arrangements to form higher-order networks and regulate cellular functions. Common examples include the formation of lamellipodia and filopodia at the cell's leading edge by actin reorganization in a migrating cell. The microvilli on the brush border epithelial cells are also formed through the F-actin network.
The high-order actin networks...
Assembly of Cytoskeletal Filaments01:18

Assembly of Cytoskeletal Filaments

Cytoskeletal filaments are polymeric forms of smaller protein subunits. However, individual cytoskeletal filaments may easily disassemble or associate with other similar filaments to form rigid structures. Microfilaments, made of actin monomers, rely on actin-binding proteins to form bundles and create networks of individual actin filaments. Microtubules rely on microtubule-associated proteins (MAPs) to form sturdy cylindrical structures. However, the proteins involved in forming complex...
Generation of Straight or Branched Actin Filaments01:14

Generation of Straight or Branched Actin Filaments

The straight or branched structure formation of actin filaments is controlled by nucleating proteins such as the formins and Arp2/3 complex. Formin-mediated assembly results in straight filaments, whereas Arp2/3 protein complex-mediated assembly results in branched actin filaments.
Arp2/3 Complex
Arp2/3 complex is a seven-subunit complex consisting of two proteins similar to actin- Arp2 and Arp3, and five other subunits that help keep Arp2 and Arp3 inactive. When required, the complex is...
Mechanism of Filopodia Formation01:39

Mechanism of Filopodia Formation

Filopodia are thin, actin-rich cellular protrusions that play an important role in many fundamental cellular functions. They vary in their occurrence, length, and positioning in different cell types, suggesting their diverse roles.
Their main function is to guide migrating cells during normal tissue morphogenesis or cancer metastasis by recognizing and making initial contacts with the extracellular matrix. However, they can also act as stationary cell anchors or help to establish communication...

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Updated: Jun 27, 2026

ECM Protein Nanofibers and Nanostructures Engineered Using Surface-initiated Assembly
16:33

ECM Protein Nanofibers and Nanostructures Engineered Using Surface-initiated Assembly

Published on: April 17, 2014

Fibrillin assembly requires fibronectin.

Laetitia Sabatier1, Daliang Chen, Christine Fagotto-Kaufmann

  • 1Faculty of Medicine, Department of Anatomy and Cell Biology, McGill University, Montreal, QC, Canada H3A 2B2.

Molecular Biology of the Cell
|November 28, 2008
PubMed
Summary
This summary is machine-generated.

Fibrillin-1 assembly into microfibrils requires extracellular fibronectin. This interaction is crucial for proper extracellular matrix formation and function, impacting conditions like Marfan syndrome.

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Using Microfluidics and Fluorescence Microscopy to Study the Assembly Dynamics of Single Actin Filaments and Bundles
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Last Updated: Jun 27, 2026

ECM Protein Nanofibers and Nanostructures Engineered Using Surface-initiated Assembly
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Fabrication of a Biomimetic Nano-Matrix with Janus Base Nanotubes and Fibronectin for Stem Cell Adhesion
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Using Microfluidics and Fluorescence Microscopy to Study the Assembly Dynamics of Single Actin Filaments and Bundles
08:02

Using Microfluidics and Fluorescence Microscopy to Study the Assembly Dynamics of Single Actin Filaments and Bundles

Published on: May 5, 2022

Area of Science:

  • Extracellular matrix biology
  • Molecular cell biology
  • Connective tissue research

Background:

  • Fibrillins form essential microfibrils in extracellular matrices.
  • Dysfunctional microfibrils are linked to Marfan syndrome and fibrillinopathies.
  • Understanding fibrillin assembly is key to matrix integrity.

Purpose of the Study:

  • To investigate the assembly mechanisms of fibrillin-1.
  • To determine the role of other matrix proteins in fibrillin-1 assembly.
  • To elucidate the molecular interactions between fibrillin and fibronectin.

Main Methods:

  • siRNA knockdown in human dermal fibroblasts.
  • Immunolabeling at light and electron microscopy levels.
  • Protein-binding assays and mapping studies.

Main Results:

  • Fibrillin-1 assembly is dependent on extracellular fibronectin fibrils.
  • Fibrillin-1 colocalizes with fibronectin during early assembly stages.
  • Fibronectin interacts with multimerized C-terminal regions of fibrillins, primarily via fibronectin type I domains (FNI(6)-FNI(9)).

Conclusions:

  • Extracellular fibronectin is essential for fibrillin-1 microfibril assembly.
  • Specific interactions between multimerized fibrillin C-termini and fibronectin mediate assembly.
  • These findings provide insights into extracellular matrix formation and fibrillinopathies.