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

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 Integrins01:15

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 events provide an effective stimulus.
Integrins01:10

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,...
Anchoring Junctions01:03

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:...
Selectins01:25

Selectins

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, which...
Laminins are the Adhesive Proteins of Basal Lamina00:55

Laminins are the Adhesive Proteins of Basal Lamina

Laminins are heterotrimeric proteins with high molecular mass found in the extracellular matrix. Each laminin molecule is composed of three chains, viz. alpha, beta, and gamma, coded by five, four, and three paralogous genes, respectively. Laminins are categories based on the compositions of the three chains.
In humans, the five forms of alpha chains are LAMA 1, LAMA 2, LAMA 3, LAMA 4, and LAMA 5. The four forms of beta chains are LAMB 1, LAMB 2, LAMB 3, and LAMB 4. The three forms of gamma...

You might also read

Related Articles

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

Sort by
Same author

A Cross-sectional Study on Quality of Life in EB: Validation of the Italian QOLEB and Assessment in Italian Patients.

Acta dermato-venereologica·2026
Same author

DOT1L Shapes ncPRC1-Target Gene Repression to Maintain Germinal Center B Cell Identity of Diffuse Large B cell Lymphoma.

Blood·2026
Same author

Maternal anti-HPA-1a antibodies block αIIbβ3/αvβ3 integrin activation, and blockade correlates with FNAIT disease severity.

Blood·2026
Same author

Melanomas and Mesenchymal Tumors Arising in Giant Congenital Melanocytic Nevi: Clinico-Pathological and Molecular Characterization of a Case Series.

Pigment cell & melanoma research·2026
Same author

C3G deregulation uncovers a dual role in B-cell lymphoma: tumor suppression and enhanced metastasis via Rap1 and Rac2 signaling.

Cell communication and signaling : CCS·2025
Same author

A single-chain derivative of an integrin-activating antibody potentiates organoid growth in Matrigel and collagen hydrogels.

Nature biotechnology·2025

Related Experiment Video

Updated: May 10, 2026

Efficient Production and Purification of Recombinant Murine Kindlin-3 from Insect Cells for Biophysical Studies
13:52

Efficient Production and Purification of Recombinant Murine Kindlin-3 from Insect Cells for Biophysical Studies

Published on: March 19, 2014

Kindlin-1 regulates integrin dynamics and adhesion turnover.

Coert Margadant1, Maaike Kreft, Giovanna Zambruno

  • 1Division of Cell Biology, The Netherlands Cancer Institute, Amsterdam, The Netherlands.

Plos One
|June 19, 2013
PubMed
Summary

Kindler syndrome arises from kindlin-1 gene mutations. This study reveals kindlin-1 regulates integrin trafficking and cell adhesion, crucial for skin integrity and function.

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

A Flow Cytometry-Based High-Throughput Technique for Screening Integrin-Inhibitory Drugs
04:15

A Flow Cytometry-Based High-Throughput Technique for Screening Integrin-Inhibitory Drugs

Published on: February 2, 2024

Related Experiment Videos

Last Updated: May 10, 2026

Efficient Production and Purification of Recombinant Murine Kindlin-3 from Insect Cells for Biophysical Studies
13:52

Efficient Production and Purification of Recombinant Murine Kindlin-3 from Insect Cells for Biophysical Studies

Published on: March 19, 2014

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

A Flow Cytometry-Based High-Throughput Technique for Screening Integrin-Inhibitory Drugs
04:15

A Flow Cytometry-Based High-Throughput Technique for Screening Integrin-Inhibitory Drugs

Published on: February 2, 2024

Area of Science:

  • Cell Biology
  • Dermatology
  • Genetics

Background:

  • Kindler syndrome is a genetic disorder caused by loss-of-function mutations in the kindlin-1 gene.
  • Integrins are crucial for cell adhesion, migration, and survival, and their function is regulated by co-activators like kindlins.

Purpose of the Study:

  • To investigate the cellular and molecular mechanisms underlying Kindler syndrome.
  • To elucidate the specific role of kindlin-1 in regulating β1 integrin function and cell behavior.

Main Methods:

  • Generation and characterization of a novel kindlin-1-deficient keratinocyte cell line from a Kindler syndrome patient.
  • Analysis of cell morphology, adhesion, spreading, focal adhesion assembly, migration, and β1 integrin expression and glycosylation.
  • Reconstitution experiments with wild-type and mutant kindlin-1.

Main Results:

  • Kindler syndrome patient cells exhibit reduced β1 integrin function, abnormal morphology, adhesion, spreading, and migration, despite kindlin-2 expression.
  • Kindlin-2 partially compensates for kindlin-1 loss, but its depletion exacerbates defects.
  • Aberrant β1 integrin glycosylation and reduced cell-surface expression were observed in patient cells.
  • Restoration with wild-type kindlin-1 normalized β1 integrin expression, glycosylation, and cellular functions, unlike a β1-binding defective mutant.

Conclusions:

  • Kindlin-1 plays a critical role in regulating β1 integrin trafficking, cell-surface expression, and adhesion turnover.
  • Kindlin-1 is essential for maintaining normal keratinocyte morphology, adhesion, and migration.
  • These findings provide new insights into the pathogenesis of Kindler syndrome and the function of kindlins in integrin regulation.