Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

Integrins

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,...

Intracellular Signaling Affects Focal Adhesions

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...

Activation of Integrins

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...

Catenins

Catenins

Catenins are characterized by multiple binding domains and dynamic structures that allow them to function as linker proteins in cell junction complexes. All catenins, except α-catenin, contain a characteristic protein sequence called the armadillo repeat and are therefore also called armadillo proteins.
Catenins in Cell Junctions
Catenins bind to cell adhesion molecules such as cadherins and link them to different cytoskeletal proteins depending on the type of cell junction. At the...

Anchoring Junctions

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:...

Tension Response at Adherens Junctions

Tension Response at Adherens Junctions

The adherens junctions that anchor cells together are multi-protein complexes that dynamically adapt to mechanical stimuli such as tensile forces and shear stress. Mechanosensory proteins in these junctions can sense such mechanical stimuli and undergo a shift in their conformation, resulting in an altered function — a process called mechanotransduction.
α-Catenin as a Mechanosensory Protein
The α-catenin of adherens junctions is an allosteric protein with three VH (vinculin...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by

Same author

In Memoriam: Richard O. Hynes (1944-2026).

Matrix biology : journal of the International Society for Matrix Biology·2026

Same author

A novel fibronectin-binding peptide reveals dynamic intermediate structures during matrix assembly.

Scientific reports·2025

Same author

Fibronectin matrix assembly at a glance.

Journal of cell science·2025

Same author

Increased basal fibronectin is sufficient to promote excess endothelial cell matrix assembly causing localized barrier dysfunction.

Molecular biology of the cell·2024

Same author

Identification of a fibronectin-binding protein signature associated with idiopathic pulmonary fibrosis.

Cells & development·2024

Same author

Extracellular matrix composition affects outgrowth of dendrites and dendritic spines on cortical neurons.

Frontiers in cellular neuroscience·2023

Search research articles

Related Experiment Video

Updated: Apr 21, 2026

The C. elegans Intestine As a Model for Intercellular Lumen Morphogenesis and In Vivo Polarized Membrane Biogenesis at the Single-cell Level: Labeling by Antibody Staining, RNAi Loss-of-function Analy

The C. elegans Intestine As a Model for Intercellular Lumen Morphogenesis and In Vivo Polarized Membrane Biogenesis at the Single-cell Level: Labeling by Antibody Staining, RNAi Loss-of-function Analy

Published on: October 3, 2017

α Integrin cytoplasmic tails have tissue-specific roles during C. elegans development.

Christopher M Meighan¹, Jean E Schwarzbauer

¹Department of Molecular Biology and Chemistry, Christopher Newport University, Newport News, VA, USA.

The International Journal of Developmental Biology

|October 31, 2014

Summary

The alpha integrin cytoplasmic tails dictate distinct cellular functions during development. Tail swapping experiments in C. elegans reveal tissue-specific roles for integrin signaling in development.

More Related Videos

Visualizing Neuroblast Cytokinesis During C. elegans Embryogenesis

Visualizing Neuroblast Cytokinesis During C. elegans Embryogenesis

Published on: March 12, 2014

In Vitro Reconstitution of Spatial Cell Contact Patterns with Isolated Caenorhabditis elegans Embryo Blastomeres and Adhesive Polystyrene Beads

In Vitro Reconstitution of Spatial Cell Contact Patterns with Isolated Caenorhabditis elegans Embryo Blastomeres and Adhesive Polystyrene Beads

Published on: November 26, 2019

Related Experiment Videos

Last Updated: Apr 21, 2026

The C. elegans Intestine As a Model for Intercellular Lumen Morphogenesis and In Vivo Polarized Membrane Biogenesis at the Single-cell Level: Labeling by Antibody Staining, RNAi Loss-of-function Analy

The C. elegans Intestine As a Model for Intercellular Lumen Morphogenesis and In Vivo Polarized Membrane Biogenesis at the Single-cell Level: Labeling by Antibody Staining, RNAi Loss-of-function Analy

Published on: October 3, 2017

Visualizing Neuroblast Cytokinesis During C. elegans Embryogenesis

Visualizing Neuroblast Cytokinesis During C. elegans Embryogenesis

Published on: March 12, 2014

In Vitro Reconstitution of Spatial Cell Contact Patterns with Isolated Caenorhabditis elegans Embryo Blastomeres and Adhesive Polystyrene Beads

In Vitro Reconstitution of Spatial Cell Contact Patterns with Isolated Caenorhabditis elegans Embryo Blastomeres and Adhesive Polystyrene Beads

Published on: November 26, 2019

Area of Science:

Cell Biology
Developmental Biology
Genetics

Background:

Integrin signaling is crucial for development, with complexity arising from multiple integrin heterodimers.
Separation of signals from different integrin types is essential within cells.

Purpose of the Study:

To investigate the role of alpha integrin cytoplasmic tails in developmental processes.
To determine how distinct alpha integrin tails influence cellular behaviors in a tissue-specific manner.

Main Methods:

Utilized chimeric alpha integrins in C. elegans to swap cytoplasmic tails between INA-1 and PAT-2.
Assessed the functional rescue of developmental defects in integrin mutants by chimeric integrins.
Examined the effects of chimeric integrins in a wild-type background.

Main Results:

A chimeric INA-1 integrin with the PAT-2 tail rescued lethality and neuron fasciculation but not all developmental processes.
A chimeric PAT-2 integrin with the INA-1 tail showed limited rescue of a PAT-2 mutation and induced defects in wild-type animals.
Alpha integrin cytoplasmic tails demonstrated distinct and context-dependent roles in cell migration, muscle organization, and survival.

Conclusions:

Alpha integrin cytoplasmic tails are key determinants of specific cellular functions during development.
The impact of integrin tails is modulated by tissue type and genetic background.
Understanding integrin tail function is vital for deciphering complex developmental signaling pathways.