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Published on: April 2, 2020
Focal adhesion kinase signaling in unexpected places
Elizabeth G Kleinschmidt1, David D Schlaepfer1
1Biomedical Sciences Graduate Program, University of California, San Diego, CA, United States; Moores Cancer Center, Department of Reproductive Medicine, 3855 Health Sciences Drive, MC 0983, La Jolla, CA 92093-0983, United States.
Abstract:
Focal adhesion kinase (FAK) is a cytoplasmic protein-tyrosine kinase first identified at extracellular matrix and integrin receptor cell adhesion sites and is a key regulator of cell movement. FAK is activated by a variety of stimuli. Herein, we discuss advances in conformational-associated FAK activation and dimerization mechanisms. Additionally, new roles have emerged for FAK signaling at cell adhesions, adherens junctions, endosomes, and the nucleus. In light of these new findings, we review how FAK activation at these sites is connected to the regulation of integrin recycling-activation, vascular permeability, cell survival, and transcriptional regulation, respectively. Studies uncovering FAK signaling connections in unexpected places within cells have yielded important new regulatory insights in cell biology.
Insights
Focal adhesion kinase (FAK) regulates cell movement and is activated through conformational changes. New research reveals FAK
Area of Science:
- Cell Biology
- Molecular Biology
- Biochemistry
Background:
- Focal adhesion kinase (FAK) is a cytoplasmic protein-tyrosine kinase.
- FAK is primarily known as a key regulator of cell movement, initially identified at cell adhesion sites.
- FAK activation is triggered by diverse stimuli.
Purpose of the Study:
- To discuss recent advances in understanding FAK activation mechanisms, including conformational changes and dimerization.
- To review novel roles of FAK signaling in various cellular compartments.
- To connect FAK activation at these sites to specific cellular processes.
Main Methods:
- Review of recent scientific literature on FAK signaling.
- Analysis of studies investigating FAK conformational dynamics and dimerization.
- Examination of research on FAK localization and function in different cellular compartments.
Main Results:
- FAK activation involves conformational changes and dimerization.
- FAK signaling extends beyond cell adhesions to adherens junctions, endosomes, and the nucleus.
- FAK activation in these locations regulates integrin recycling, vascular permeability, cell survival, and gene transcription.
Conclusions:
- FAK plays multifaceted roles in cellular regulation, extending beyond its canonical functions.
- Understanding FAK signaling in diverse cellular locations provides new insights into cell biology.
- Further research into FAK's mechanisms and roles is crucial for understanding cellular processes.
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