ArticleMolecular and cellular biology2010
Nemo-like kinase, an essential effector of anterior formation, functions downstream of p38 mitogen-activated protein kinase.
Article in Molecular and cellular biology, 2010. 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, 21 citations in OpenAlex.
- Gene expression analysis of the Tao kinase family of Ste20p-like map kinase kinase kinases during early embryonic development in Xenopus laevis.Gene expression patterns : GEP · 2023Article
- Diamond Blackfan anemia is mediated by hyperactive Nemo-like kinase.Nature communications · 2020Article
- Nemo-like kinase reduces mutant huntingtin levels and mitigates Huntington's disease.Human molecular genetics · 2020Article
- Mechanism for neurotransmitter-receptor matching.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Sishen WanFrontiers in pharmacology · 2019Article
- NLK functions to maintain proliferation and stemness of NSCLC and is a target of metformin.Journal of hematology & oncology · 2015Article
- Association of nuclear-localized Nemo-like kinase with heat-shock protein 27 inhibits apoptosis in human breast cancer cells.PloS one · 2014Article
- Nemo-like kinase associated with proliferation and apoptosis by c-Myb degradation in breast cancer.PloS one · 2013Article
- IQGAP1 functions as a modulator of dishevelled nuclear localization in Wnt signaling.PloS one · 2013Article
- Article
- Homodimerization of Nemo-like kinase is essential for activation and nuclear localization.Molecular biology of the cell · 2011Article
- Morpholino gene knockdown in adult Fundulus heteroclitus: role of SGK1 in seawater acclimation.PloS one · 2011Article
Corrections and comments
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Authors and funding
9 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Nemo-like kinase (NLK) is known to function as a mitogen-activated protein kinase (MAPK)-like kinase. However, the upstream molecules and molecular mechanisms that regulate NLK activity remain unclear. In the present study, we identified p38 MAPK as an upstream kinase and activator of NLK. p38 regulates the function of NLK via phosphorylation, and this modification can be abrogated by depletion of endogenous p38. In Xenopus laevis embryos, depletion of either p38beta or NLK by antisense morpholino oligonucleotides results in a severe defect in anterior development and impaired expression of endogenous anterior markers. It is notable that morphants of Xenopus p38alpha, another isoform of the p38 MAPK family, exhibited no obvious defects in anterior development. Defects in head formation or in the expression of anterior marker genes caused by suppression of endogenous p38beta expression could be rescued by expression of wild-type NLK but not by expression of mutant NLK lacking the p38beta phosphorylation site. In contrast, defects in head formation or in the expression of anterior marker genes caused by suppression of endogenous NLK expression could not be rescued by expression of p38. These results provide the first evidence that p38 specifically regulates NLK function, which is required for anterior formation in Xenopus development.
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