ArticleMolecular and cellular biology2015
JAK2 tyrosine kinase phosphorylates and is negatively regulated by centrosomal protein Ninein.
Article in Molecular and cellular biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 15 citations in OpenAlex.
- Centrosomal JAK2 Tyrosine Kinase Regulates Primary Cilia Length, Cell Proliferation, and Cilia Orientation During Cell Migration.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2026Article
- JAK2-CHK2 signaling safeguards the integrity of the mitotic spindle assembly checkpoint and genome stability.Cell death & disease · 2022Article
- JAK2 gene knockout inhibits corneal allograft rejection in mice by regulating dendritic cell-induced T cell immune tolerance.Cell death discovery · 2022Article
- The SH2 domain and kinase activity of JAK2 target JAK2 to centrosome and regulate cell growth and centrosome amplification.PloS one · 2022Article
- Casein kinase TbCK1.2 regulates division of kinetoplast DNA, and movement of basal bodies in the African trypanosome.PloS one · 2021Article
- Knockdown of GSG2 inhibits prostate cancer progression in vitro and in vivo.International journal of oncology · 2020Article
- Phosphorylation of multiple proteins involved in ciliogenesis by Tau Tubulin kinase 2.Molecular biology of the cell · 2020Article
- Neuroprotective potential of imatinib in global ischemia-reperfusion-induced cerebral injury: possible role of Janus-activated kinase 2/signal transducer and activator of transcription 3 and connexin 43.The Korean journal of physiology & pharmacology : official journal of the Korean Physiological Society and the Korean Society of Pharmacology · 2020Article
- Article
- AG490, a JAK2-specific inhibitor, downregulates the expression and activity of organic anion transporter-3.Journal of pharmacological sciences · 2018Article
- Genomic diagnostics within a medically underserved population: efficacy and implications.Genetics in medicine : official journal of the American College of Medical Genetics · 2018Article
- C14orf166 overexpression correlates with tumor progression and poor prognosis of breast cancer.Journal of translational medicine · 2016Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
JAK2 is a cytoplasmic tyrosine kinase critical for cytokine signaling. In this study, we have identified a novel centrosome-associated complex containing ninein and JAK2. We have found that active JAK2 localizes around the mother centrioles, where it partly colocalizes with ninein, a protein involved in microtubule (MT) nucleation and anchoring. We demonstrated that JAK2 is an important regulator of centrosome function. Depletion of JAK2 or use of JAK2-null cells causes defects in MT anchoring and increased numbers of cells with mitotic defects; however, MT nucleation is unaffected. We showed that JAK2 directly phosphorylates the N terminus of ninein while the C terminus of ninein inhibits JAK2 kinase activity in vitro. Overexpressed wild-type (WT) or C-terminal (amino acids 1179 to 1931) ninein inhibits JAK2. This ninein-dependent inhibition of JAK2 significantly decreases prolactin- and interferon gamma (IFN-γ)-induced tyrosyl phosphorylation of STAT1 and STAT5. Downregulation of ninein enhances JAK2 activation. These results indicate that JAK2 is a novel member of centrosome-associated complex and that this localization regulates both centrosomal function and JAK2 kinase activity, thus controlling cytokine-activated molecular pathways.
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