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Related Concept Videos

Fibronectins Connect Cells with ECM01:25

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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.
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Fibrous proteins are either long and narrow proteins or assemble to form long and thin structures. They contain repetitive units and usually consist of either alpha helices or beta sheets and, in rare cases, a mix of both. The amino acids in the primary structure often consist of repeating amino acid sequences. The role of fibrous proteins is primarily structural. Many are located in the extracellular matrix and are present in connective tissues to impart strength and joint mobility. They are...
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Many proteins can be classified into two distinct subtypes - globular or fibrous. These two types differ in their shapes and solubilities.
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Structural Protein Function01:56

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Structural proteins are a category of proteins responsible for functions ranging from cell shape and movement to providing support to major structures such as bones, cartilage, hair, and muscles. This group includes proteins such as collagen, actin, myosin, and keratin.
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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.
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Anchoring Junctions01:03

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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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Related Experiment Video

Updated: Mar 21, 2026

ECM Protein Nanofibers and Nanostructures Engineered Using Surface-initiated Assembly
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Dynamic structure of plasma fibronectin.

Lisa M Maurer1, Wenjiang Ma1, Deane F Mosher1

  • 1a Departments of Biomolecular Chemistry and Medicine , University of Wisconsin-Madison , Madison , WI , United States.

Critical Reviews in Biochemistry and Molecular Biology
|May 18, 2016
PubMed
Summary

Plasma fibronectin, a large glycoprotein, transitions from a compact to an extended conformation. Biophysical and structural studies reveal how module interactions maintain its structure and how binding events perturb it.

Keywords:
Bacterial adhesinfibronectinfibronectin type I modulefibronectin type II modulefibronectin type III moduleheparan sulfateintegrinplasma proteinsyndecan

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Biophysics

Background:

  • Fibronectin is a large vertebrate glycoprotein involved in diverse cellular processes.
  • It exists as a dimer of subunits, each composed of multiple modules (type I, II, and III).
  • Plasma fibronectin circulates in a compact form before extending upon cell surface binding for fibril assembly.

Purpose of the Study:

  • To review biophysical and structural studies on plasma fibronectin conformation changes.
  • To elucidate the mechanisms underlying the transition from compact to extended states.
  • To identify interactions maintaining fibronectin structure and how binding events affect it.

Main Methods:

  • Review of biophysical and structural studies.
  • Analysis of Nuclear Magnetic Resonance (NMR) and crystallography data.
  • Examination of module-module interactions and flexible sequences.

Main Results:

  • Fibronectin modules (type I, II, III) possess stable secondary and tertiary structures.
  • Flexible sequences are present at the N-terminus, C-terminus, and between specific modules.
  • Specific module-module interactions stabilize the compact quaternary structure of circulating fibronectin.
  • Binding events, such as cell surface or bacterial adhesin binding, perturb this quaternary structure.

Conclusions:

  • Plasma fibronectin's conformation is regulated by module interactions and flexible linkers.
  • The transition to an extended conformation is crucial for its biological functions, including fibril assembly.
  • Understanding these structural dynamics is key to comprehending fibronectin's role in cellular adhesion and bacterial interactions.