ArticleMolecular and cellular biochemistry2011
Phosphorylation of Caldesmon by PFTAIRE1 kinase promotes actin binding and formation of stress fibers.
Article in Molecular and cellular biochemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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9 citing papers in PubMed, 17 citations in OpenAlex.
- Cytoplasmic Localization Isoform of Cyclin Y Enhanced the Metastatic Ability of Lung CancerFrontiers in cell and developmental biology · 2021Article
- Downregulation of PFTK1 Inhibits Migration and Invasion of Non-Small Cell Lung Cancer.OncoTargets and therapy · 2020Article
- Reorganization of the Vimentin Network in Smooth Muscle.Journal of engineering and science in medical diagnostics and therapy · 2019Article
- The roles and regulation of the actin cytoskeleton, intermediate filaments and microtubules in smooth muscle cell migration.Respiratory research · 2017Review
- PFTK1 Promotes Gastric Cancer Progression by Regulating Proliferation, Migration and Invasion.PloS one · 2015Article
- Quantitative proteomic analysis in HCV-induced HCC reveals sets of proteins with potential significance for racial disparity.Journal of translational medicine · 2013Article
- Deregulations in the cyclin-dependent kinase-9-related pathway in cancer: implications for drug discovery and development.ISRN oncology · 2013Article
- Overexpression of PFTK1 predicts resistance to chemotherapy in patients with oesophageal squamous cell carcinoma.British journal of cancer · 2012Article
- Imatinib mesylate causes genome-wide transcriptional changes in systemic sclerosis fibroblasts in vitro.Clinical and experimental rheumatologyArticle
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Caldesmon (CaD) is an actin-binding protein that is capable of stabilizing actin filaments. Phosphorylation of CaD is widely accepted in the actin cytoskeletal modeling and promotion of cell migration. In this study, we show that CaD is a downstream phosphorylation substrate of PFTK1, a novel Cdc-2-related ser/thr protein kinase. Our study stemmed from an earlier investigation where we demonstrated that PFTK1 kinase conferred cell migratory advantages in human hepatocellular carcinoma (HCC) cells. Here, we showed that PFTK1-knockdown cells exhibited much reduced CaD phosphorylation and consequently caused dissociation of CaD from the F-actin fibers. The cellular localization of CaD was also altered in the absence of PFTK1. Immunofluorescence analysis revealed that PFTK1-abrogated cells exhibited a diffused and blurred appearance of CaD localization, whereas intact co-localization with F-actins was apparent in PFTK1-expressing cells. Without the binding of CaD to actin, disappearance of actin stress fibers was also evident in PFTK1-abrogated cells. In addition, we found that CaD is also commonly up-regulated in HCC tumors when compared to adjacent non-malignant liver (P = 0.022). Taken together, our results highlight a novel biological cascade that involved the phosphorylation activation of CaD by PFTK1 kinase in promoting formation of actin stress fibers.
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