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

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...

Cadherins in Tissue Organization

Cadherins in Tissue Organization

The cadherins are a superfamily of cell adhesion molecules comprising over 180 variants, with specific tissues expressing a particular combination of cadherin types. Cadherins generally exhibit homophilic binding; i.e., cadherins on one cell bind to cadherins of the same or closely related type on another cell. Thus, cells of the same type have a specific affinity to bind to each other and sort themselves into clusters to form tissues.
Cell Sorting During Development
Cell sorting plays an...

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 adherens...

The JAK-STAT Signaling Pathway

The JAK-STAT Signaling Pathway

Several cytokine receptors have tightly bound Janus kinase or JAK proteins attached at their cytosolic tail. Small signaling molecules such as cytokines, growth hormones, or prolactins bind to the cytokine receptors and initiate their dimerization. The dimerization brings the cytosolic JAKs together that trans-phosphorylate and activates each other. The activated JAKs now phosphorylate cytosolic tails of the cytokine receptors, which serve as binding sites for adaptor proteins such as SH2...

MAPK Signaling Cascades

MAPK Signaling Cascades

Mitogen-activated protein kinase, or MAPK pathway, activates three sequential kinases to regulate cellular responses such as proliferation, differentiation, survival, and apoptosis. The canonical MAPK pathway starts with a mitogen or growth factor binding to an RTK. The activated RTKs stimulate Ras, which recruits Raf or MAP3 Kinase (MAPKKK), the first kinase of the MAPK signaling cascade. Raf further phosphorylates and activates MEK or MAP2 Kinases (MAPKK), which in turn phosphorylates MAP...

Adherens Junctions

Adherens Junctions

Strong contact points between adjacent cells anchor them to each other, forming tissues. Such anchoring junctions are of two types – adherens junctions and desmosomes. Adherens junctions are abundant in tissues such as epithelium and endothelium, forming a continuous zone of adhesion called the adhesion belt. In other tissues, such as heart muscle, they appear as clusters, linking the cells to produce coordinated heart muscle contraction.
Adherens Junctions are Dynamic
The endothelial cells...

You might also read

Related Articles

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

Sort by

Same author

Estrogen receptor alpha and beta chromatin interactions govern ovarian folliculogenesis but dissipate during ovulation.

Endocrinology·2026

Same author

HIF-2α expression is controlled by the progesterone receptor and regulates hCG-induced gene expression in granulosa cells during ovulation in mice.

Molecular and cellular endocrinology·2026

Same author

Dual inhibition of carbonic anhydrase IX and glutathione peroxidase 4 as a novel strategy for ferroptosis-induced tumor cell death.

European journal of medicinal chemistry·2025

Same author

Neutrophil extracellular trap gene expression signatures identify prognostic and targetable signaling axes for inhibiting pancreatic tumour metastasis.

Communications biology·2025

Same author

Drug tolerance and persistence to EGFR inhibitor treatment are mediated by an ILK-SFK-YAP signaling axis in lung adenocarcinoma.

Oncogene·2025

Same author

Identification of intratumoral bacteria that enhance breast tumor metastasis.

mBio·2025

Search research articles

Related Experiment Video

Updated: Jul 2, 2026

Bead Aggregation Assays for the Characterization of Putative Cell Adhesion Molecules

Bead Aggregation Assays for the Characterization of Putative Cell Adhesion Molecules

Published on: October 17, 2014

Integrin-linked kinase regulates E-cadherin expression through PARP-1.

Timothy R McPhee¹, Paul C McDonald, Arusha Oloumi

¹Genetics Graduate Program, Department of Biochemistry and Molecular Biology, University of British Columbia, Vancouver, British Columbia, Canada.

Developmental Dynamics : an Official Publication of the American Association of Anatomists

|September 6, 2008

Summary

Integrin-Linked Kinase (ILK) controls E-cadherin expression via Poly(ADP-ribose) polymerase-1 (PARP-1). ILK regulates PARP-1 binding to the Snail promoter, impacting epithelial to mesenchymal transition and cancer progression.

More Related Videos

Visualization and Quantitative Analysis of Genotoxin-Induced PARP1/PARP2 Activation in Cells Using a Fluorescent Fusion Protein-Based Reporter

Visualization and Quantitative Analysis of Genotoxin-Induced PARP1/PARP2 Activation in Cells Using a Fluorescent Fusion Protein-Based Reporter

Published on: April 17, 2026

An Immunofluorescent Method for Characterization of Barrett’s Esophagus Cells

An Immunofluorescent Method for Characterization of Barrett’s Esophagus Cells

Published on: July 20, 2014

Related Experiment Videos

Last Updated: Jul 2, 2026

Bead Aggregation Assays for the Characterization of Putative Cell Adhesion Molecules

Bead Aggregation Assays for the Characterization of Putative Cell Adhesion Molecules

Published on: October 17, 2014

Visualization and Quantitative Analysis of Genotoxin-Induced PARP1/PARP2 Activation in Cells Using a Fluorescent Fusion Protein-Based Reporter

Visualization and Quantitative Analysis of Genotoxin-Induced PARP1/PARP2 Activation in Cells Using a Fluorescent Fusion Protein-Based Reporter

Published on: April 17, 2026

An Immunofluorescent Method for Characterization of Barrett’s Esophagus Cells

An Immunofluorescent Method for Characterization of Barrett’s Esophagus Cells

Published on: July 20, 2014

Area of Science:

Cell Biology
Molecular Oncology
Biochemistry

Background:

E-cadherin repression by Snail is crucial for epithelial to mesenchymal transition (EMT) and cancer progression.
Integrin-Linked Kinase (ILK) is a potential regulator of cellular processes involved in cancer.

Purpose of the Study:

To elucidate the role of ILK in regulating E-cadherin expression.
To identify the signaling pathway through which ILK affects E-cadherin and EMT.

Main Methods:

Overexpression and silencing of ILK, Akt, and Snail in Scp2 and PC3 cell lines.
Identification of Snail promoter ILK Responsive Element (SIRE) binding proteins using biochemical assays.
Analysis of PARP-1 binding to SIRE and its effect on Snail and ZEB1 expression.

Main Results:

ILK overexpression stimulated Snail expression and decreased E-cadherin.
Silencing ILK, Akt, or Snail led to E-cadherin re-expression.
PARP-1 was identified as a SIRE-binding protein; ILK silencing inhibited this binding.
PARP-1 silencing reduced Snail and ZEB1, upregulating E-cadherin.

Conclusions:

ILK represses E-cadherin expression by regulating PARP-1.
PARP-1 binding to the Snail promoter (SIRE) is a key mechanism modulated by ILK.
This ILK-PARP-1-Snail axis represents a novel regulatory pathway in EMT and cancer.