![]() ![]() The Author(s) under exclusive licence to The Genetics Society of Korea. In addition, we confirmed that the inactivation of JNK1 K55N mutant significantly reduced the JNK1-mediated phosphorylation of OTX2 by performing an immune complex protein kinase assay.Ĭ-Jun N-terminal kinase 1 (JNK1) phosphorylates OTX2 transcription factor through the protein-protein interaction.ĭevelopment JNK1 OTX2 Phosphorylation Protein–protein interaction Retina. The protein-protein interaction and co-localization between JNK1 and OTX2 were further validated in the developing P0 mouse retina. JNK1 directly interacted with OTX2 through the transactivation domain at the c-terminal region. In vivo and in vitro kinase assay of JNK1 was performed to detect the phosphorylation of OTX2 by JNK1. Therefore, JNKs represent attractive oncogenic targets for cancer. It is increasingly clear that the continuous activation of JNKs has a role in cancer development and progression. The protein interaction between JNK1 and OTX2 was identified with the co-immunoprecipitation and immunocytochemistry. The JNKs are members of mitogen-activated protein kinases (MAPK) which regulate many physiological processes including inflammatory responses, macrophages, cell proliferation, differentiation, survival, and death. TGF-I (Transforming Growth Factor-beta), JNK (c-Jun terminal kinase). which can be upregulated by bone morphogenetic proteins 2 (BMP2). Data detailed in 'Regulation of protein turnover by longevity pathways' have been. To identify the binding partner of OTX2, we performed co-immunoprecipitation and detected with a pooled antibody that targeted effective kinases. c-Jun N-terminal kinase 1 negatively regulates osteoblastic differentiation induced by BMP2 via phosphorylation of Runx2 at Ser104. The identification of JNK1 as an OTX2 regulatory protein through the protein interaction and phosphorylation. However, the regulatory mechanisms of OTX2 are poorly identified. The transcription factor orthodenticle homeobox 2 (OTX2) has critical functions in brain and eye development, and its mutations in humans are related to retinal diseases, such as ocular coloboma and microphthalmia. ![]()
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