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    Nlk nemo like kinase [ Mus musculus (house mouse) ]

    Gene ID: 18099, updated on 18-Sep-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    Reduction of nemo-like kinase increases lysosome biogenesis and ameliorates TDP-43-related neurodegeneration.

    Reduction of nemo-like kinase increases lysosome biogenesis and ameliorates TDP-43-related neurodegeneration.
    Tejwani L, Jung Y, Kokubu H, Sowmithra S, Ni L, Lee C, Sanders B, Lee PJ, Xiang Y, Luttik K, Soriano A, Yoon J, Park J, Ro HH, Ju H, Liao C, Tieze SM, Rigo F, Jafar-Nejad P, Lim J., Free PMC Article

    08/19/2023
    Nemo-like kinase reduces mutant huntingtin levels and mitigates Huntington's disease.

    Nemo-like kinase reduces mutant huntingtin levels and mitigates Huntington's disease.
    Jiang M, Zhang X, Liu H, LeBron J, Alexandris A, Peng Q, Gu H, Yang F, Li Y, Wang R, Hou Z, Arbez N, Ren Q, Dong JL, Whela E, Wang R, Ratovitski T, Troncoso JC, Mori S, Ross CA, Lim J, Duan W., Free PMC Article

    08/7/2021
    Diamond Blackfan anemia is mediated by hyperactive Nemo-like kinase.

    Diamond Blackfan anemia is mediated by hyperactive Nemo-like kinase.
    Wilkes MC, Siva K, Chen J, Varetti G, Youn MY, Chae H, Ek F, Olsson R, Lundbäck T, Dever DP, Nishimura T, Narla A, Glader B, Nakauchi H, Porteus MH, Repellin CE, Gazda HT, Lin S, Serrano M, Flygare J, Sakamoto KM., Free PMC Article

    08/29/2020
    The phosphatase activity of WIP1 increases Wnt activity through Nemo-like kinase (NLK). WIP1 directly interacted with NLK, which is highly homologous to p38 MAPK, a WIP1 substrate, and dephosphorylated its activation site.

    Wip1 directly dephosphorylates NLK and increases Wnt activity during germ cell development.
    Cho SJ, Cha BS, Kwon OS, Lim J, Shin DM, Han DW, Ishitani T, Jho EH, Fornace AJ, Cha HJ.

    03/16/2019
    our data suggest that NLK/Nemo acts as an endogenous regulator of Hippo signaling by controlling nuclear localization and activity of YAP/Yorkie.

    Phosphorylation by NLK inhibits YAP-14-3-3-interactions and induces its nuclear localization.
    Moon S, Kim W, Kim S, Kim Y, Song Y, Bilousov O, Kim J, Lee T, Cha B, Kim M, Kim H, Katanaev VL, Jho EH., Free PMC Article

    08/19/2017
    NLK is a novel signaling molecule for proper lung development through the interconnection between epithelial and endothelial cells during lung morphogenesis

    Nemo-like kinase regulates the expression of vascular endothelial growth factor (VEGF) in alveolar epithelial cells.
    Ke H, Masoumi KC, Ahlqvist K, Seckl MJ, Rydell-Törmänen K, Massoumi R., Free PMC Article

    04/8/2017
    NLK can phosphorylate the mutant polyglutamine-expanded androgen receptor protein, enhance its aggregation, and promote androgen receptor-dependent gene transcription by regulating androgen receptor-cofactor interactions.

    Nemo-like kinase is a novel regulator of spinal and bulbar muscular atrophy.
    Todd TW, Kokubu H, Miranda HC, Cortes CJ, La Spada AR, Lim J., Free PMC Article

    07/2/2016
    Nlk is a negative regulator of skeletal homeostasis.

    Nemo-like kinase regulates postnatal skeletal homeostasis.
    Canalis E, Kranz L, Zanotti S., Free PMC Article

    09/27/2014
    either reducing NLK enzymatic activity or decreasing NLK expression levels can have beneficial effects against the toxicity induced by polyglutamine-expanded ATXN1

    Polyglutamine disease toxicity is regulated by Nemo-like kinase in spinocerebellar ataxia type 1.
    Ju H, Kokubu H, Todd TW, Kahle JJ, Kim S, Richman R, Chirala K, Orr HT, Zoghbi HY, Lim J., Free PMC Article

    07/27/2013
    NEMO binding domain peptide treatment results in improved generation of specific force and greater resistance to lengthening activations in dystrophic diaphragm muscle ex vivo.

    Systemic delivery of NEMO binding domain/IKKγ inhibitory peptide to young mdx mice improves dystrophic skeletal muscle histopathology.
    Reay DP, Yang M, Watchko JF, Daood M, O'Day TL, Rehman KK, Guttridge DC, Robbins PD, Clemens PR., Free PMC Article

    05/26/2012
    Nlk suppresses osteoblastogenesis by opposing BMP/Smad and WNT canonical signaling

    Nemo-like kinase inhibits osteoblastogenesis by suppressing bone morphogenetic protein and WNT canonical signaling.
    Zanotti S, Canalis E., Free PMC Article

    05/5/2012
    Wnt3a stimulation led to an increase in the interaction of TAB2 with NLK and the formation of a TAK1.TAB2.NLK complex, suggesting that this TAK1-TAB2-NLK pathway may constitute a negative feedback mechanism for canonical Wnt signaling.

    TAB2 scaffolds TAK1 and NLK in repressing canonical Wnt signaling.
    Li M, Wang H, Huang T, Wang J, Ding Y, Li Z, Zhang J, Li L., Free PMC Article

    05/31/2010
    NLK negatively regulates osteoblastic differentiation.

    Nemo-like kinase (NLK) expression in osteoblastic cells and suppression of osteoblastic differentiation.
    Nifuji A, Ideno H, Ohyama Y, Takanabe R, Araki R, Abe M, Noda M, Shibuya H.

    05/10/2010
    NLK negatively regulates Notch-dependent transcriptional activation by phosphorylating Notch1ICD. Phosphorylated Notch1ICD is impaired in its ability to form a transcriptionally active ternary complex.

    Nemo-like kinase suppresses Notch signalling by interfering with formation of the Notch active transcriptional complex.
    Ishitani T, Hirao T, Suzuki M, Isoda M, Ishitani S, Harigaya K, Kitagawa M, Matsumoto K, Itoh M.

    04/19/2010
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