Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Intracellular Signaling Affects Focal Adhesions01:17

Intracellular Signaling Affects Focal Adhesions

3.4K
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...
3.4K
Activation of Integrins01:15

Activation of Integrins

4.9K
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...
4.9K
Role of Ephrin-Eph Signalling in Intestinal Stem Cell Renewal01:22

Role of Ephrin-Eph Signalling in Intestinal Stem Cell Renewal

2.6K
Erythropoietin-producing hepatocellular carcinoma receptor (Eph) and its ligand, Eph receptor-interacting protein (Ephrin) were first discovered in the human carcinoma cell line, hence the name. Ephrin-Eph interaction guides cells to reach their appropriate location in adult tissues. They also play an essential role in the immune system by helping in immune cell migration, adhesion, and activation. Based on their structure and function, Eph is divided into two classes — EphA and EphB.
2.6K
Integrins01:10

Integrins

5.2K
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,...
5.2K
Anchoring Junctions01:03

Anchoring Junctions

4.8K
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:...
4.8K
Selectins01:25

Selectins

4.1K
Cell adhesion is  an essential aspect of multicellularity. While stable cell interactions usually occur between cells of the same type, transient cell interactions occur between cells of different tissue types, such as between neutrophils and endothelial cells. Selectins are one class of cell adhesion molecules (CAMs) that bind carbohydrate ligands to form transient cell adhesion. They are rod-like proteins with a long extracellular part of variable length ending with the lectin domain,...
4.1K

You might also read

Related Articles

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

Sort by
Same author

TPGS1 regulates central spindle microtubule glutamylation and remodeling during telophase and abscission.

EMBO reports·2026
Same author

Semaphorin-7A promotes macrophage-mediated mammary epithelial and ductal carcinoma in situ invasion.

Breast cancer research : BCR·2025
Same author

Ubiquitylation-dependent Rap2 activation regulates lamellipodia dynamics during cell migration.

Journal of cell science·2025
Same author

TPGS1 Regulates Central Spindle Microtubule Glutamylation and Remodeling During Telophase and Abscission.

bioRxiv : the preprint server for biology·2025
Same author

Rap1 activity and localization is regulated by Rab40/CRL5 facilitated mono-ubiquitylation.

microPublication biology·2025
Same author

Semaphorin-7A promotes macrophage-mediated mammary epithelial and ductal carcinoma in situ invasion.

Research square·2025

Related Experiment Video

Updated: Jan 11, 2026

Author Spotlight: Development of a Method for Identifying Small Molecular Antagonists of β2 Integrin Activation
04:15

Author Spotlight: Development of a Method for Identifying Small Molecular Antagonists of β2 Integrin Activation

Published on: February 2, 2024

2.3K

Checking in with EPLIN: EPLINα as a regulator of integrin trafficking.

Andrew Neumann1, Rytis Prekeris1

  • 1Department of Cell and Developmental Biology, School of Medicine, University of Colorado Anschutz Medical Campus, Aurora, CO 80045, USA.

Developmental Cell
|November 18, 2025
PubMed
Summary

EPLINα isoform localizes to Rab21-positive endosomes, regulating β1-integrin recycling. This finding is crucial for understanding cell-matrix adhesion, migration, and cancer progression.

More Related Videos

Static Adhesion Assay for the Study of Integrin Activation in T Lymphocytes
09:14

Static Adhesion Assay for the Study of Integrin Activation in T Lymphocytes

Published on: June 13, 2014

16.7K
An In Vitro Assay to Study Platelet Migration Using RGD-Functionalized Avidin-Biotin Tethers
05:43

An In Vitro Assay to Study Platelet Migration Using RGD-Functionalized Avidin-Biotin Tethers

Published on: November 8, 2024

773

Related Experiment Videos

Last Updated: Jan 11, 2026

Author Spotlight: Development of a Method for Identifying Small Molecular Antagonists of β2 Integrin Activation
04:15

Author Spotlight: Development of a Method for Identifying Small Molecular Antagonists of β2 Integrin Activation

Published on: February 2, 2024

2.3K
Static Adhesion Assay for the Study of Integrin Activation in T Lymphocytes
09:14

Static Adhesion Assay for the Study of Integrin Activation in T Lymphocytes

Published on: June 13, 2014

16.7K
An In Vitro Assay to Study Platelet Migration Using RGD-Functionalized Avidin-Biotin Tethers
05:43

An In Vitro Assay to Study Platelet Migration Using RGD-Functionalized Avidin-Biotin Tethers

Published on: November 8, 2024

773

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Cancer Research

Background:

  • Cell-to-matrix adhesion is vital for cellular functions.
  • Integrin recycling regulates cell adhesion and migration.
  • EPLIN proteins are involved in actin cytoskeleton organization.

Purpose of the Study:

  • To investigate the localization and function of the EPLINα isoform.
  • To elucidate the role of EPLINα in β1-integrin recycling.
  • To understand EPLINα's contribution to cell migration and cancer progression.

Main Methods:

  • Immunofluorescence microscopy to determine EPLINα localization.
  • Biochemical assays to assess β1-integrin recycling.
  • Cell migration assays.
  • Analysis of cancer cell lines.

Main Results:

  • EPLINα specifically localizes to Rab21-positive endosomes.
  • EPLINα is essential for efficient β1-integrin recycling.
  • EPLINα influences cell-matrix adhesion and cell migration.
  • Altered EPLINα levels impact cancer cell progression.

Conclusions:

  • EPLINα's unique localization dictates its function in β1-integrin recycling.
  • EPLINα plays a significant role in regulating cell adhesion and migration.
  • EPLINα is a potential therapeutic target for cancer treatment.