Engagement of DYRK2 in proper control for cell division

Nihira, Naoe Taira; Yoshida, Kiyotsugu

doi:10.1080/15384101.2015.1007751

Cited by 34 publications

(30 citation statements)

References 27 publications

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“…Ser46 phosphorylation triggers the induction of apoptosis-related genes, as shown in Figure 1 phosphorylation of p53 at Ser46 by DYRK2 regulates apoptotic cell death in response to DNA damage. 1,19 Previous findings also showed that p53 was phosphorylated by PKCδ in MCF7 and U2OS cells upon exposure to genotoxic agents ( Figure 4). 7 PKCδ-mediated phosphorylation was required for the interaction of PKCδ with p53.…”

Section: Ser46 a Major Phosphorylation Site For Apoptosismentioning

confidence: 72%

Tumor suppressive role for kinases phosphorylating p53 in DNA damage‐induced apoptosis

2018

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Tumor suppressor p53 plays an important role in cancer prevention. Under normal conditions, p53 is maintained at a low level. However, in response to various cellular stresses, p53 is stabilized and activated, which, in turn, initiates DNA repair, cell‐cycle arrest, senescence and apoptosis. Post‐translational modifications of p53 including phosphorylation, ubiquitination, and acetylation at multiple sites are important to regulate its activation and subsequent transcriptional gene expression. Particularly, phosphorylation of p53 plays a critical role in modulating its activation to induce apoptosis in cancer cells. In this context, previous studies show that several serine/threonine kinases regulate p53 phosphorylation and downstream gene expression. The molecular basis by which p53 and its kinases induce apoptosis for cancer prevention has been extensively studied. However, the relationship between p53 phosphorylation and its kinases and how the activity of kinases is controlled are still largely unclear; hence, they need to be investigated. In this review, we discuss various roles for p53 phosphorylation and its responsible kinases to induce apoptosis and a new therapeutic approach in a broad range of cancers.

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Section: Ser46 a Major Phosphorylation Site For Apoptosismentioning

confidence: 72%

Tumor suppressive role for kinases phosphorylating p53 in DNA damage‐induced apoptosis

2018

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“…Dual-specificity tyrosine-phosphorylation-regulated kinase 2 (DYRK2) is a Ser/Thr kinase that plays key roles in the regulation of proliferation, cell differentiation and survival [26]. DYRK2 contributes to the regulation of various signalling pathways via the phosphorylation of relevant proteins such as NFAT, p53, c-Jun, c-Myc, eIF2Bε, tau, hPXR, glycogen synthase, CRMP4, 4E-BP1, Snail, katanin and SIAH2 [26][27][28][29][30]. Several studies highlighted the importance of DYRK2 impairing the development and progression of human cancers, such as non-small cell lung cancer, esophageal adenocarcinomas, breast cancer and ovarian serous adenocarcinoma [31][32][33][34].…”

Section: Introductionmentioning

confidence: 99%

Phosphorylation-dependent regulation of the NOTCH1 intracellular domain by dual-specificity tyrosine-regulated kinase 2

Morrugares

Correa-Sáez

Moreno

et al. 2019

Cell. Mol. Life Sci.

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NOTCH proteins constitute a receptor family with a widely conserved role in cell cycle, growing and development regulation. NOTCH1, the best characterised member of this family, regulates the expression of key genes in cell growth and angiogenesis, playing an essential role in cancer development. These observations provide a relevant rationale to propose the inhibition of the intracellular domain of NOTCH1 (Notch1-IC) as a strategy for treating various types of cancer. Notch1-IC stability is mainly controlled by post-translational modifications. FBXW7 ubiquitin E3 ligase-mediated degradation is considered one of the most relevant, being the previous phosphorylation at Thr-2512 residue required. In the present study, we describe for the first time a new regulation mechanism of the NOTCH1 signalling pathway mediated by DYRK2. We demonstrate that DYRK2 phosphorylates Notch1-IC in response to chemotherapeutic agents and facilitates its proteasomal degradation by FBXW7 ubiquitin ligase through a Thr-2512 phosphorylation-dependent mechanism. We show that DYRK2 regulation by chemotherapeutic agents has a relevant effect on the viability, motility and invasion capacity of cancer cells expressing NOTCH1. In summary, we reveal a novel mechanism of regulation for NOTCH1 which might help us to better understand its role in cancer biology.

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“…). DYRK2 is a tumour suppressor by phosphorylating a pro‐apoptotic protein p53 for inducing apoptosis‐related genes and for degrading a key protein, snail, for tumour metastasis (Nihira & Yoshida ). Collectively, DYRKs among different species and kingdoms function in a broad spectrum of cell growth and developmental processes.…”

Section: Introductionmentioning

confidence: 99%

“…For example, an extra allele of DYRK1Awas found associated with defective neural development in Down syndrome (Wegiel et al 2011), and mice with haploinsufficiency in DYRK1A showed reduced brain size and abnormal brain morphology (Fotaki et al 2002). DYRK2 is a tumour suppressor by phosphorylating a proapoptotic protein p53 for inducing apoptosis-related genes and for degrading a key protein, snail, for tumour metastasis (Nihira & Yoshida 2015). Collectively, DYRKs among different species and kingdoms function in a broad spectrum of cell growth and developmental processes.…”

Section: Introductionmentioning

confidence: 99%

Plant dual‐specificity tyrosine phosphorylation‐regulated kinase optimizes light‐regulated growth and development in Arabidopsis

Huang

et al. 2017

Plant Cell & Environment

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Light controls vegetative and reproductive development of plants. For a plant, sensing the light input properly ensures coordination with the ever-changing environment. Previously, we found that LIGHT-REGULATED WD1 (LWD1) and LWD2 regulate the circadian clock and photoperiodic flowering. Here, we identified Arabidopsis YET ANOTHER KINASE1 (AtYAK1), an evolutionarily conserved protein and a member of dual-specificity tyrosine phosphorylation-regulated kinases (DYRKs), as an interacting protein of LWDs. Our study revealed that AtYAK1 is an important regulator for various light responses, including the circadian clock, photomorphogenesis and reproductive development. AtYAK1 could antagonize the function of LWDs in regulating the circadian clock and photoperiodic flowering. By examining phenotypes of atyak1, we found that AtYAK1 regulated light-induced period-length shortening and photomorphogenic development. Moreover, AtYAK1 mediated plant fertility especially under inferior light conditions including low light and short-day length. This study discloses a new regulator connecting environmental light to plant growth.

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Engagement of DYRK2 in proper control for cell division

Cited by 34 publications

References 27 publications

Tumor suppressive role for kinases phosphorylating p53 in DNA damage‐induced apoptosis

Tumor suppressive role for kinases phosphorylating p53 in DNA damage‐induced apoptosis

Phosphorylation-dependent regulation of the NOTCH1 intracellular domain by dual-specificity tyrosine-regulated kinase 2

Plant dual‐specificity tyrosine phosphorylation‐regulated kinase optimizes light‐regulated growth and development in Arabidopsis

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