ArticleCardiovascular research2010
Role of FRNK tyrosine phosphorylation in vascular smooth muscle spreading and migration.
Article in Cardiovascular research, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 21 citations in OpenAlex.
- Focal adhesion kinase-related non-kinase ameliorates liver fibrosis by inhibiting aerobic glycolysisWorld journal of gastroenterology · 2022Article
- Regulation of Focal Adhesion Kinase through a Direct Interaction with an Endogenous Inhibitor.Biochemistry · 2017Article
- Effects of integrin α5β1 on the proliferation and migration of human aortic vascular smooth muscle cells.Molecular medicine reports · 2016Article
- Antibody ligation of human leukocyte antigen class I molecules stimulates migration and proliferation of smooth muscle cells in a focal adhesion kinase-dependent manner.Human immunology · 2011Article
- Focal adhesion kinase-related nonkinase inhibits vascular smooth muscle cell invasion by focal adhesion targeting, tyrosine 168 phosphorylation, and competition for p130(Cas) binding.Arteriosclerosis, thrombosis, and vascular biology · 2011Article
- FRNK inhibition of focal adhesion kinase-dependent signaling and migration in vascular smooth muscle cells.Arteriosclerosis, thrombosis, and vascular biology · 2010Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
aimsFocal adhesion kinase (FAK) and its autonomously expressed, C-terminal inhibitor FAK-related non-kinase (FRNK), are important regulators of vascular smooth muscle cell (VSMC) spreading and migration. However, the mechanisms of FRNK-mediated inhibition of FAK-dependent signalling are not fully defined. The aim of this study was to determine the potential role of FRNK tyrosine phosphorylation in regulating these processes. METHODS AND
resultsRat carotid arteries were balloon-injured and FAK and FRNK expression and phosphorylation were examined by immunocytochemistry, immunoprecipitation, and western blotting with total and phosphospecific antibodies. FAK and FRNK expression increased four- and nine-fold, respectively, in alpha-smooth muscle actin-positive VSMCs of injured arteries when compared with contralateral control arteries, and the upregulated FRNK was phosphorylated at residues Y168 and Y232. In A7r5 cells (an embryonic rat VSMC line), endogenously expressed FRNK was also phosphorylated at Y168 and Y232 under basal conditions, and Y168/Y232 phosphorylation increased in response to angiotensin II treatment. When overexpressed in A7r5 cells and adult rat aortic smooth muscle cells (RASM), wild-type (wt) GFP-tagged FRNK was also phosphorylated at residues Y168 and Y232, and GFP-wtFRNK inhibited cell spreading and migration. Mutation of GFP-FRNK at Y168 (GFP-Y168F-FRNK) abrogated FRNK-mediated inhibition of cell spreading and migration, but did not affect its localization in VSMC focal adhesions or its ability to inhibit FAK tyrosine phosphorylation.
conclusionPhosphorylation of Y168 on FRNK may represent a novel mechanism by which FRNK inhibits cell spreading and migration in VSMCs.
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