CaMK‐II promotes focal adhesion turnover and cell motility by inducing tyrosine dephosphorylation of FAK and paxillin
Open accessAbstract
Transient elevations in Ca 2+ have previously been shown to promote focal adhesion disassembly and cell motility through an unknown mechanism. In this study, evidence is provided to show that CaMK‐II, a Ca 2+/calmodulin dependent protein kinase, influences fibroblast adhesion and motility. TIRF microscopy reveals a dynamic population of CaMK‐II at the cell surface in migrating cells. Inhibition of CaMK‐II with two mechanistically distinct, membrane permeant inhibitors (KN‐93 and myr‐AIP) freezes lamellipodial dynamics, accelerates spreading on fibronectin, enlarges paxillin‐containing focal adhesions and blocks cell motility. In contrast, constitutively active CaMK‐II is not found at the cell surface, reduces cell attachment, eliminates paxillin from focal adhesions and decreases the phospho‐tyrosine levels of both FAK and paxillin; all of these events can be reversed with myr‐AIP. Thus, both CaMK‐II inhibition and constitutive activation block cell motility through over‐stabilization or destabilization of focal adhesions, respectively. Coupled with the existence of transient Ca 2+ elevations and a dynamic CaMK‐II population, these findings provide the first direct evidence that CaMK‐II enables cell motility by transiently and locally stimulating tyrosine dephosphorylation of focal adhesion proteins to promote focal adhesion turnover. Cell Motil. Cytoskeleton, 2008. © 2008 Wiley‐Liss, Inc.
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Upon mechanical activation, Piezo1 mediates Ca2+ influx, which can promote FAK phosphorylation via Ca2+-dependent mechanisms (e.g., calmodulin/CaMKII-mediated regulation) in other cell types.
“Upon mechanical activation, Piezo1 mediates Ca2+ influx, which can promote FAK phosphorylation via Ca2+-dependent mechanisms (e.g., calmodulin/CaMKII-mediated regulation), as reported in other cell types.99,100”
From Mechanosensitive calcium ion channels Piezo1: A therapeutic target in liver disease (2025) · cites this paper as [99]
The Discussion reports that another study found CaMK-II-mediated phosphorylation of FAK at S843 after G-protein receptor activation. It does not connect that mechanism to mechanical activation or Piezo1-mediated Ca2+ influx. Under this paper’s own experimental conditions, CaMK-II did not alter FAK S843 phosphorylation and instead reduced FAK phospho-tyrosine levels. (LLM, conf=0.87)
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CaMKII promotes ROS-dependent apoptosis induced by Suilysin in PK-15 cellsPreprint
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- Authors
- Easley, C. A., Brown, C. M., Horwitz, A. F., & Tombes, R. M.
- Affiliations
- Virginia Commonwealth University (US)
- McGill University (CA)
- University of Virginia (US)
- Corresponding author
- Tombes, Robert M.
- Venue
- Cell Motility
- Publisher
- Wiley
- Published
- 2008-07-08
- Volume
- 65
- Issue
- 8
- Pages
- 662-674
- ISSN
- 0886-1544 (ISSN-L)
- PMC
- PMC2830206
- OpenAlex
- W2117554463
- Cited by
- 56
- References
- 69
- Citations by year
- 2025: 4 · 2023: 3 · 2022: 1 · 2021: 1 · 2020: 3 · 2019: 1 · 2018: 4 · 2017: 2 · 2016: 3 · 2015: 4 · 2014: 3 · 2013: 5 · 2012: 5
- FWCI
- 3.68
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Cell Motility and the Cytoskeleton (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institute of General Medical Sciences (R37GM023244)
- Topics
- Health Sciences › Medicine › Immunology and Allergy › Cell Adhesion Molecules Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular Mechanics and Interactions
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Keywords
- CaMKII, focal adhesion turnover, cell motility, tyrosine dephosphorylation, focal adhesion kinase, paxillin, calcium signaling, lamellipodia, fibroblast adhesion, cell spreading, KN-93
- MeSH terms
- Benzenesulfonamides, Animals, Benzylamines, Cell Movement, Fibronectins, Microscopy, Fluorescence, Phosphoproteins, Sulfonamides, Tyrosine, Immunoblotting, Calcium-Calmodulin-Dependent Protein Kinases, Focal Adhesions, NIH 3T3 Cells, Protein Kinase Inhibitors, Mice, Focal Adhesion Protein-Tyrosine Kinases, Paxillin
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