ArticleHaematologica2011
Multiple oligomerization domains of KANK1-PDGFRβ are required for JAK2-independent hematopoietic cell proliferation and signaling via STAT5 and ERK.
Article in Haematologica, 2011. 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, 22 citations in OpenAlex.
- PDGFRβ in Stem Cell Microenvironments: Cross-Tissue Evidence and Hypotheses for the Limbal Stem Cell Niche.Stem cells international · 2026Review
- Kinase regulation by liquid-liquid phase separation.Trends in cell biology · 2023Review
- Therapeutic Advances of Rare ALK Fusions in Non-Small Cell Lung Cancer.Current oncology (Toronto, Ont.) · 2022Review
- The genetic landscape of pancreatic head ductal adenocarcinoma in China and prognosis stratification.BMC cancer · 2022Article
- ALK Fusion Partners Impact Response to ALK Inhibition: Differential Effects on Sensitivity, Cellular Phenotypes, and Biochemical Properties.Molecular cancer research : MCR · 2018Article
- PDGF-induced fibroblast growth requires monounsaturated fatty acid production by stearoyl-CoA desaturase.FEBS open bio · 2017Article
- Kank2 activates talin, reduces force transduction across integrins and induces central adhesion formation.Nature cell biology · 2016Article
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- The tyrosine phosphatase SHP2 is required for cell transformation by the receptor tyrosine kinase mutants FIP1L1-PDGFRα and PDGFRα D842V.Molecular oncology · 2014Article
- Transcription factors in late megakaryopoiesis and related platelet disorders.Journal of thrombosis and haemostasis : JTH · 2013Review
- Review of current classification, molecular alterations, and tyrosine kinase inhibitor therapies in myeloproliferative disorders with hypereosinophilia.Journal of blood medicine · 2013Article
- ETV6-PDGFRB and FIP1L1-PDGFRA stimulate human hematopoietic progenitor cell proliferation and differentiation into eosinophils: the role of nuclear factor-κB.Haematologica · 2012Article
- Hepatitis C virus-host interactions: Etiopathogenesis and therapeutic strategies.World journal of experimental medicine · 2012Article
- Tyrosine kinase gene fusions in cancer: translating mechanisms into targeted therapies.Journal of cellular and molecular medicine · 2012Review
- Platelet-derived growth factors and their receptors in normal and malignant hematopoiesis.American journal of blood research · 2012Article
- PDGF: the nuts and bolts of signalling toolbox.Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2011Review
Corrections and comments
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Authors and funding
7 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundKANK1-PDGFRB is a fusion gene generated by the t(5;9) translocation between KANK1 and the platelet-derived growth factor receptor beta gene PDGFRB. This hybrid was identified in a myeloproliferative neoplasm featuring severe thrombocythemia, in the absence of the JAK2 V617F mutation. DESIGN AND
methodsKANK1-PDGFRB was transduced into Ba/F3 cells and CD34(+) human progenitor cells to gain insights into the mechanisms whereby this fusion gene transforms cells.
resultsAlthough platelet-derived growth factor receptors are capable of activating JAK2, KANK1-PDGFRβ did not induce JAK2 phosphorylation in hematopoietic cells and a JAK inhibitor did not affect KANK1-PDGFRβ-induced cell growth. Like JAK2 V617F, KANK1-PDGFRβ constitutively activated STAT5 transcription factors, but this did not require JAK kinases. In addition KANK1-PDGFRβ induced the phosphorylation of phospholipase C-γ, ERK1 and ERK2, like wild-type PDGFRβ and TEL-PDGFRβ, another hybrid protein found in myeloid malignancies. We next tested various mutant forms of KANK1-PDGFRβ in Ba/F3 cells and human CD34(+) hematopoietic progenitors. The three coiled-coil domains located in the N-terminus of KANK1 were required for KANK1-PDGFRβ-induced cell growth and signaling via STAT5 and ERK. However, the coiled-coils were not essential for KANK1-PDGFRβ oligomerization, which could be mediated by another new oligomerization domain. KANK1-PDGFRβ formed homotrimeric complexes and heavier oligomers.
conclusionsKANK1-PDGFRB is a unique example of a thrombocythemia-associated oncogene that does not signal via JAK2. The fusion protein is activated by multiple oligomerization domains, which are required for signaling and cell growth stimulation.
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