ArticleCell communication and signaling : CCS2014
Downstream signaling and genome-wide regulatory effects of PTK7 pseudokinase and its proteolytic fragments in cancer cells.
Article in Cell communication and signaling : CCS, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 30 citations in OpenAlex.
- Recent insights into the therapeutic strategies targeting the pseudokinase PTK7 in cancer.Oncogene · 2024Review
- PTK7: an underestimated contributor to human cancer.Frontiers in oncology · 2024Review
- Senescent cells perturb intestinal stem cell differentiation through Ptk7 induced noncanonical Wnt and YAP signaling.Nature communications · 2023Article
- Whole-Exome Sequencing Identifies a Novel Germline Variant inInternational journal of molecular sciences · 2022Article
- The Mutational Landscape ofGenes · 2021Article
- Ptk7 Is Dynamically Localized at Neural Crest Cell-Cell Contact Sites and Functions in Contact Inhibition of Locomotion.International journal of molecular sciences · 2021Article
- Interleukin-15 response signature predicts RhCMV/SIV vaccine efficacy.PLoS pathogens · 2021Article
- ENST00000489707.5 Is a Preferred Alternative Splicing Variant of PTK7 in Adrenocortical Cancer and Shows Potential Prognostic Value.Medical science monitor : international medical journal of experimental and clinical research · 2019Article
- The Increased PTK7 Expression Is a Malignant Factor in Cervical Cancer.Disease markers · 2019Article
- Periostin secreted by cancer-associated fibroblasts promotes cancer stemness in head and neck cancer by activating protein tyrosine kinase 7.Cell death & disease · 2018Article
- Matrix metalloproteinases - From the cleavage data to the prediction tools and beyond.Biochimica et biophysica acta. Molecular cell research · 2017Review
- Review
- Proteolytic cleavage, trafficking, and functions of nuclear receptor tyrosine kinases.The FEBS journal · 2015Review
- SAR Studies of Exosite-Binding Substrate-Selective Inhibitors of A Disintegrin And Metalloprotease 17 (ADAM17) and Application as Selective in Vitro Probes.Journal of medicinal chemistry · 2015Article
- Article
- Role of TM4SF1 in regulating breast cancer cell migration and apoptosis through PI3K/AKT/mTOR pathway.International journal of clinical and experimental pathology · 2015Article
- PTK7 protein is decreased in epithelial ovarian carcinomas with poor prognosis.International journal of clinical and experimental pathology · 2014Article
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
Abstract
backgroundThe full-length membrane protein tyrosine kinase 7 (PTK7) pseudokinase, an important component of the planar cell polarity and the Wnt canonical and non-canonical pathways, is a subject of step-wise proteolysis in cells and tissues. The proteolysis of PTK7 involves membrane type-matrix metalloproteinase (MT1-MMP), members of the Disintegrin Domain and Metalloproteinase (ADAM) family, and γ-secretase. This multi-step proteolysis results in the generation of the digest fragments of PTK7. These fragments may be either liberated into the extracellular milieu or retained on the plasma membrane or released into the cytoplasm and then transported into the nucleus.
resultsWe employed the genome-wide transcriptional and kinome array analyses to determine the role of the full-length membrane PTK7 and its proteolytic fragments in the downstream regulatory mechanisms, with an emphasis on the cell migration-related genes and proteins. Using fibrosarcoma HT1080 cells stably expressing PTK7 and its mutant and truncated species, the structure of which corresponded to the major PTK7 digest fragments, we demonstrated that the full-length membrane 1-1070 PTK7, the N-terminal 1-694 soluble ectodomain fragment, and the C-terminal 622-1070 and 726-1070 fragments differentially regulate multiple genes and signaling pathways in our highly invasive cancer cell model. Immunoblotting of the selected proteins were used to validate the results of our high throughput assays.
conclusionsOur results suggest that PTK7 levels need to be tightly controlled to enable migration and that the anti-migratory effect of the full-length membrane PTK7 is linked to the down-regulation of multiple migration-related genes and to the activation of the Akt and c-Jun pathway. In turn, the C-terminal fragments of PTK7 act predominantly via the RAS-ERK and CREB/ATF1 pathway and through the up-regulation of cadherin-11. In general, our data correlate well with the distinct functionality of the full-length receptor tyrosine kinases and their respective intracellular domain (ICD) proteolytic fragments.
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