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Related Concept Videos

Tight Junctions01:29

Tight Junctions

Tight junctions are molecular seals between cells that prevent the leaking of fluids, ions, and other small solutes across cavities and compartments in multicellular organisms. They are mainly composed of claudin and occludin transmembrane proteins, and other proteins such as tricellulin and JAM (junctional adhesion molecule). All these proteins are 4-pass transmembrane proteins, except JAM, which is a single-pass transmembrane protein belonging to the immunoglobulin superfamily. The...
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...
Mechanisms of Membrane Domain Formation00:59

Mechanisms of Membrane Domain Formation

Different physical properties of lipids and proteins allow them to localize and form distinct islands or domains in the membrane. Some membrane domains are formed due to protein-protein interactions, whereas others are formed due to the presence of specific lipids such as sphingolipids and sterols—for example, large proteins, such as bacteriorhodopsin, aggregate and create distinct domains.
Another mechanism for membrane domain formation involves membrane proteins interacting with cytoskeletal...
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...
Mechanism of Lamellipodia Formation01:31

Mechanism of Lamellipodia Formation

Cells migrating in response to external stimuli form lamellipodia, which are thin membrane protrusions supported by a mesh of linked, branched, or unbranched actin filaments. These actin filaments interact with myosin motor proteins, creating the dynamic actomyosin complex within the cytoskeleton. Contractility, or the ability to generate contractile stress, is inherent to the actomyosin complex. It helps cells detect the stiffness of the surrounding ECM and exert contractile force for...
Cancer Cell Migration through Invadopodia01:35

Cancer Cell Migration through Invadopodia

Invadosome is a broad category of cell surface structures with proteolytic activity that  degrades the extracellular matrix (ECM). Invadosomes are present in normal cell types, including macrophages, endothelial cells, and neurons, as well as tumor cells. Although the macrophage podosomes and tumor cell invadopodia are classified as invadosomes, they have different structures, molecular pathways, and functions. Podosomes are short structures that last for a few minutes. However, invadopodia can...

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Related Experiment Video

Updated: Jun 8, 2026

Biological Preparation and Mechanical Technique for Determining Viscoelastic Properties of Zonular Fibers
06:39

Biological Preparation and Mechanical Technique for Determining Viscoelastic Properties of Zonular Fibers

Published on: December 16, 2021

Zona occludens proteins modulate podosome formation and function.

Joachim Kremerskothen1, Miriam Stölting, Christiane Wiesner

  • 1Department for Molecular Nephrology, Internal Medicine D, University Clinic Münster, Domagkstrasse 3a, Münster, Germany 48149. joachim.kremerskothen@uni-muenster.de

FASEB Journal : Official Publication of the Federation of American Societies for Experimental Biology
|October 9, 2010
PubMed
Summary
This summary is machine-generated.

Zona occludens protein 1 (ZO-1) is newly identified in podosomes, regulating cell adhesion and matrix remodeling. Reduced ZO-1 impairs podosome formation and extracellular matrix degradation.

More Related Videos

Quantitative Measurement of Invadopodia-mediated Extracellular Matrix Proteolysis in Single and Multicellular Contexts
14:23

Quantitative Measurement of Invadopodia-mediated Extracellular Matrix Proteolysis in Single and Multicellular Contexts

Published on: August 27, 2012

Related Experiment Videos

Last Updated: Jun 8, 2026

Biological Preparation and Mechanical Technique for Determining Viscoelastic Properties of Zonular Fibers
06:39

Biological Preparation and Mechanical Technique for Determining Viscoelastic Properties of Zonular Fibers

Published on: December 16, 2021

Quantitative Measurement of Invadopodia-mediated Extracellular Matrix Proteolysis in Single and Multicellular Contexts
14:23

Quantitative Measurement of Invadopodia-mediated Extracellular Matrix Proteolysis in Single and Multicellular Contexts

Published on: August 27, 2012

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Podosomes are dynamic actin-rich structures crucial for cell adhesion and extracellular matrix (ECM) remodeling.
  • Cortactin is a key scaffolding protein involved in podosome biogenesis and actin assembly.
  • Zona occludens protein 1 (ZO-1) is primarily known for its role in tight junction assembly.

Purpose of the Study:

  • To investigate the role of ZO-1 and its binding partners in podosome formation and function.
  • To determine the mechanism of ZO-1 recruitment to podosomes.
  • To assess the impact of ZO-1 on podosome-mediated matrix degradation.

Main Methods:

  • Immunofluorescence microscopy to visualize ZO-1 and associated proteins in A7r5 smooth muscle cells.
  • Phorbol ester treatment to induce podosome formation.
  • Truncation studies to identify domains of ZO-1 critical for podosome localization.
  • RNA interference (RNAi) to impair ZO-1 expression.
  • Matrix degradation assays.

Main Results:

  • ZO-1 rapidly relocates to newly formed podosomes upon phorbol ester treatment in A7r5 cells.
  • ZO-1 binding partners, including l-afadin and α-catenin, are also recruited to podosomes.
  • The actin-binding domain of ZO-1, not its interaction with cortactin, is essential for podosome recruitment.
  • Reduced ZO-1 expression significantly decreases podosome formation and matrix degradation.

Conclusions:

  • ZO-1 is a novel component of podosomes, extending its known functions beyond tight junctions.
  • ZO-1 plays a critical role in regulating podosome formation and ECM remodeling.
  • ZO-1 and its associated proteins represent a new regulatory mechanism for cell adhesion and matrix degradation.