ArticleMolecular and cellular biochemistry2010
Human SMAD4 is phosphorylated at Thr9 and Ser138 by interacting with NLK.
Article in Molecular and cellular biochemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
6 citing papers in PubMed, 8 citations in OpenAlex.
- MicroRNA-663 regulates the proliferation of fibroblasts in hypertrophic scars via transforming growth factor-β1.Experimental and therapeutic medicine · 2018Article
- Aberrant expression of miR-663 and transforming growth factor-β1 in nasal polyposis in children.Experimental and therapeutic medicine · 2018Article
- Expression of TGF-β1 and miRNA-145 in patients with diabetic foot ulcers.Experimental and therapeutic medicine · 2016Article
- NLK functions to maintain proliferation and stemness of NSCLC and is a target of metformin.Journal of hematology & oncology · 2015Article
- Nemo-like kinase regulates postnatal skeletal homeostasis.Journal of cellular physiology · 2014Article
- Nemo regulates cell dynamics and represses the expression of miple, a midkine/pleiotrophin cytokine, during ommatidial rotation.Developmental biology · 2013Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Smads are important intracellular effectors in signaling pathways of the transforming growth factor-beta (TGF-beta). Receptor-activated Smads combine with a common Smad4 to translocate into the nucleus where they cooperate with other transcription factors to activate or repress transcription. SMAD4 is an important tumor suppressor gene. Smad4 has been shown to be constitutively phosphorylated, but the kinase that performs this phosphorylation is unknown. In this study, Smad4 was identified to interact with Nemo-like kinase (NLK) by a yeast two-hybrid system, and this interaction was confirmed in vitro and in vivo. Furthermore, the linker sequence of Smad4 is sufficient for this specific interaction. NLK is a conserved Ser/Thr kinase. Using in vitro kinase assays, we identified that threonine 9 (Thr9) and Serine 138 (Ser138) within the N-terminal Mad homology1 (MH1) domain of Smad4 could be phosphorylated by NLK. Our research suggests that NLK may play a novel role in the regulatory of Smad4 through phosphorylation.
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