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Updated: Jul 28, 2026

In vitro Cell Migration and Invasion Assays

In vitro Cell Migration and Invasion Assays

Published on: June 1, 2014

Focal adhesion kinase activates Stat1 in integrin-mediated cell migration and adhesion.

B Xie¹, J Zhao, M Kitagawa

¹Department of Pathology, Yale University School of Medicine, New Haven, Connecticut 06520-8023, USA.

The Journal of Biological Chemistry

|March 30, 2001

Summary

Focal adhesion kinase (FAK) activates Stat1, a signaling pathway that reduces cell adhesion and promotes cell migration. This discovery reveals a new mechanism regulating cell movement.

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Area of Science:

Cell Biology
Molecular Biology
Biochemistry

Background:

Focal adhesion kinase (FAK) plays a crucial role in cell migration.
The precise mechanisms by which FAK influences cell adhesion and migration are still being elucidated.

Purpose of the Study:

To investigate the mechanism by which FAK regulates cell adhesion and migration.
To determine if FAK activates the signal transducer and activator of transcription (STAT) pathway.

Main Methods:

Co-immunoprecipitation and in vitro binding assays were used to assess the interaction between FAK and STAT proteins.
FAK-deficient cells and cells with a C-terminal deletion of FAK (FAKDeltaC14) were utilized.
Depletion of Stat1 was performed to evaluate its role in cell adhesion and migration.

Main Results:

FAK directly activates Stat1, but not Stat3, during cell adhesion.
Stat1 transiently associates with FAK via its C-terminal domain, which is essential for FAK localization at focal contacts.
Stat1 activation is reduced in FAK-deficient cells, leading to decreased cell migration.
Depletion of Stat1 enhances cell adhesion and reduces cell migration.

Conclusions:

A novel signaling pathway involving integrin/FAK activation of Stat1 has been identified.
This pathway is critical for reducing cell adhesion and promoting cell migration.
FAK-mediated Stat1 activation represents a key regulatory mechanism in cell motility.