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

MAPK Signaling Cascades01:07

MAPK Signaling Cascades

9.2K
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...
9.2K
Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

7.1K
Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
7.1K
Inhibition of Cdk Activity02:34

Inhibition of Cdk Activity

6.2K
The orderly progression of the cell cycle depends on the activation of Cdk protein by binding to its cyclin partner. However, the cell cycle must be restricted when undergoing abnormal changes. Most cancers correlate to the deregulated cell cycle, and since Cdks are a central component of the cell cycle, Cdk inhibitors are extensively studied to develop anticancer agents. For instance, cyclin D associates with several Cdks, such as Cdk 4/6, to form an active complex. The cyclin D-Cdk4/6 complex...
6.2K
cAMP-dependent Protein Kinase Pathways01:25

cAMP-dependent Protein Kinase Pathways

9.2K
Cyclic Adenosine Monophosphate (cAMP) is an essential second messenger that activates protein kinase A (PKA) and regulates various biological processes. A single epinephrine molecule binds to GPCR and activates several heterotrimeric G proteins, each stimulating multiple adenylyl cyclase, amplifying the signal, and synthesizing large numbers of cAMP molecules. Small changes in cAMP concentration affect PKA activity. The binding of four cAMP molecules induces a conformational change in PKA,...
9.2K
Amplifying Signals via Enzymatic Cascade01:22

Amplifying Signals via Enzymatic Cascade

19.2K
When a ligand binds to a cell-surface receptor, the receptor's intracellular domain changes shape, which may either activate its enzyme function or allow its binding to other molecules. The initial signal is amplified by most signal transduction pathways. This means that a single ligand molecule can activate multiple molecules of a downstream target. Proteins that relay a signal are most commonly phosphorylated at one or more sites, activating or inactivating the protein. Kinases catalyze...
19.2K
Restarting Stalled Replication Forks02:37

Restarting Stalled Replication Forks

6.5K
DNA replication is initiated at sites containing predefined DNA sequences known as origins of replication. DNA is unwound at these sites by the minichromosome maintenance (MCM) helicase and other factors such as Cdc45 and the associated GINS complex.The unwound single strands are protected by replication protein A (RPA) until DNA polymerase starts synthesizing DNA at the 5’ end of the strand in the same direction as the replication fork. To prevent the replication fork from falling apart,...
6.5K

You might also read

Related Articles

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

Sort by
Same author

Magnetically actuated microrobotic system for sequential treatment of biofilm.

Proceedings of the National Academy of Sciences of the United States of America·2026
Same author

How balanced time perspective affects short-video addiction: a chain mediation model based on trait anxiety and ego depletion.

BMC psychology·2026
Same author

Molecular characterisation and phylogenetic placement of a new cestode, <i>Oochoristica turpanoeremiadis</i> sp. nov. (Cestoda: Cyclophyllidea: Linstowiidae), parasitising <i>Eremias roborowskii</i> from Turpan Basin in China.

Parasitology·2026
Same author

Liquid-Liquid Phase Separation in Cancer Drug Resistance: Mechanisms and Therapeutic Opportunities.

Oncology research·2026
Same author

A Real-Time Magnetic Adhesion Force Estimation Method for Wall-Climbing Robots Equipped with Halbach Permanent Magnet Arrays.

Sensors (Basel, Switzerland)·2026
Same author

Intelligent scheduling and resource allocation for urban air mobility networks based on graph neural networks.

Scientific reports·2026

Related Experiment Video

Updated: Mar 29, 2026

An In Vitro Dormancy Model of Estrogen-sensitive Breast Cancer in the Bone Marrow: A Tool for Molecular Mechanism Studies and Hypothesis Generation
08:48

An In Vitro Dormancy Model of Estrogen-sensitive Breast Cancer in the Bone Marrow: A Tool for Molecular Mechanism Studies and Hypothesis Generation

Published on: June 30, 2015

8.7K

An FAK Kinase/Scaffold Mode-Switch in Dormancy and Resistance.

Changchang Sun1, Qiuting Feng1, Yiyang Zhao1

  • 1Department of Medical Oncology, Shuguang Hospital, Shanghai University of Traditional Chinese Medicine, Shanghai 201203, China.

Cancers
|March 28, 2026
PubMed
Summary

Late relapsing cancers are driven by dormant cells. Targeting focal adhesion kinase (FAK) functional modes, not just its activity, may eliminate these persistent cells and prevent relapse.

Keywords:
Cancer dormancyDrug resistanceFocal adhesion kinase (FAK)PROTACsYes-associated protein (YAP)

More Related Videos

An In Vitro System to Study Tumor Dormancy and the Switch to Metastatic Growth
09:14

An In Vitro System to Study Tumor Dormancy and the Switch to Metastatic Growth

Published on: August 11, 2011

16.4K
Characterize Disease-related Mutants of RAF Family Kinases by Using a Set of Practical and Feasible Methods
07:49

Characterize Disease-related Mutants of RAF Family Kinases by Using a Set of Practical and Feasible Methods

Published on: July 17, 2019

6.6K

Related Experiment Videos

Last Updated: Mar 29, 2026

An In Vitro Dormancy Model of Estrogen-sensitive Breast Cancer in the Bone Marrow: A Tool for Molecular Mechanism Studies and Hypothesis Generation
08:48

An In Vitro Dormancy Model of Estrogen-sensitive Breast Cancer in the Bone Marrow: A Tool for Molecular Mechanism Studies and Hypothesis Generation

Published on: June 30, 2015

8.7K
An In Vitro System to Study Tumor Dormancy and the Switch to Metastatic Growth
09:14

An In Vitro System to Study Tumor Dormancy and the Switch to Metastatic Growth

Published on: August 11, 2011

16.4K
Characterize Disease-related Mutants of RAF Family Kinases by Using a Set of Practical and Feasible Methods
07:49

Characterize Disease-related Mutants of RAF Family Kinases by Using a Set of Practical and Feasible Methods

Published on: July 17, 2019

6.6K

Area of Science:

  • Oncology
  • Cell Biology
  • Cancer Therapeutics

Background:

  • Late relapses in cancer are often caused by dormant tumor cells and drug-tolerant persisters (DTPs).
  • Focal adhesion kinase (FAK) and YAP/TAZ are key regulators of cell survival, quiescence, and reactivation, integrating mechanical cues with stress signaling.
  • Current ATP-competitive FAK inhibitors incompletely eradicate persister cells, suggesting limitations in targeting FAK activity alone.

Purpose of the Study:

  • To propose a "Mode-Switch" model for FAK function in cancer persister cells.
  • To explain the incomplete efficacy of ATP-competitive FAK inhibitors against persister reservoirs.
  • To motivate novel therapeutic strategies targeting FAK protein stability or downstream signaling pathways.

Main Methods:

  • Conceptual framework development based on existing literature.
  • Analysis of FAK signaling in relation to cell persistence and reactivation.
  • Proposal of pathology-compatible proxies for FAK functional mode assessment (pY397-FAK/total FAK, localization, YAP/TAZ/TEAD activity).

Main Results:

  • FAK operates in at least two functional modes: Mode I (kinase-dependent, promoting regrowth) and Mode II (kinase-independent, sustaining persistence).
  • The "Mode-Switch" model explains why inhibiting FAK activity alone is insufficient to eliminate persister cells.
  • Composite readouts can potentially distinguish between these FAK functional modes.

Conclusions:

  • Targeting FAK's functional modes, rather than just its kinase activity, is crucial for eradicating cancer persister cells.
  • Strategies like FAK degradation or YAP/TEAD blockade may be effective in dismantling persister reservoirs.
  • A framework for biomarker-stratified intervention in minimal residual disease is proposed, matching therapeutic modality to dominant FAK functional mode.