Related Experiment Video

Updated: May 10, 2026

Impedance-based Real-time Measurement of Cancer Cell Migration and Invasion
09:23

Impedance-based Real-time Measurement of Cancer Cell Migration and Invasion

Published on: April 2, 2020

c-Abl Kinase Is a Regulator of αvβ3 Integrin Mediated Melanoma A375 Cell Migration

Chunmei Zhang1, Chao Yang, Ruifei Wang

  • 1Department of Cell Biology, Norman Bethune College of Medicine, Jilin University, Changchun, Jilin Province, China.

Plos One
|June 28, 2013
PubMed

Insights

The c-Abl kinase interacts with integrin αvβ3 to regulate melanoma cell migration stimulated by PDGF. This interaction is crucial for signaling pathways involving talin and affects integrin clustering and affinity.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Integrins are transmembrane receptors linking the extracellular matrix to the cytoskeleton, crucial for cell migration.
  • c-Abl kinase is a nonreceptor tyrosine kinase involved in signal transduction pathways.
  • Integrin regulation is vital for tumor cell migration, particularly in response to growth factors.

Purpose of the Study:

  • To investigate the role of c-Abl kinase in αvβ3 integrin-mediated melanoma cell migration.
  • To elucidate the mechanism by which c-Abl kinase influences αvβ3 integrin activity and clustering.

Main Methods:

  • Co-localization studies of c-Abl kinase and αvβ3 integrin in A375 melanoma cells.
  • Assessment of integrin affinity regulation by c-Abl kinase activity.
  • Analysis of protein-protein interactions involving c-Abl kinase, αvβ3 integrin, and talin.

Main Results:

  • c-Abl kinase dynamically colocalizes with αvβ3 integrin during PDGF-stimulated migration.
  • c-Abl kinase activity, induced by PDGF, regulates αvβ3 integrin clustering and affinity.
  • The interaction between c-Abl kinase and αvβ3 integrin requires the talin head domain and involves the SH3 domain of c-Abl kinase.

Conclusions:

  • c-Abl kinase plays a critical, novel role in αvβ3 integrin-mediated melanoma cell migration.
  • The interaction is dependent on c-Abl kinase activity, not ligand binding, indicating a role beyond outside-in signaling.
  • This study reveals a new regulatory mechanism for integrin function in cancer cell motility.

More Related Videos

Characterize Disease-related Mutants of RAF Family Kinases by Using a Set of Practical and Feasible Methods07:49

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

Published on: July 17, 2019

Intracellular Phosphoflow Cytometry of Acute Myeloid Leukemia Patient-Derived Xenotransplants07:38

Intracellular Phosphoflow Cytometry of Acute Myeloid Leukemia Patient-Derived Xenotransplants

Published on: June 6, 2025

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,...
Cancer Cell Migration through Invadopodia01:35

Cancer Cell Migration through Invadopodia

Invadosome is a broad category of cell surface structures with proteolytic activity that  degrades the extracellular matrix (ECM). Invadosomes are present in normal cell types, including macrophages, endothelial cells, and neurons, as well as tumor cells. Although the macrophage podosomes and tumor cell invadopodia are classified as invadosomes, they have different structures, molecular pathways, and functions. Podosomes are short structures that last for a few minutes. However, invadopodia can...
Inhibition of Cdk Activity02:34

Inhibition of Cdk Activity

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...
MAPK Signaling Cascades01:07

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...