ArticleMolecular and cellular biology2002
Phosphorylation of NFATc4 by p38 mitogen-activated protein kinases.
Article in Molecular and cellular biology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 84 papers.
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Who cites it
84 citing papers in PubMed, 175 citations in OpenAlex.
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- Physiological and Psychological Stress of Microwave Radiation-Induced Cardiac Injury in Rats.International journal of molecular sciences · 2023Article
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- Gene cascade analysis in human granulosa tumor cells (KGN) following exposure to high levels of free fatty acids and insulin.Journal of ovarian research · 2021Article
- Targeting the non-ATP-binding pocket of the MAP kinase p38γ mediates a novel mechanism of cytotoxicity in cutaneous T-cell lymphoma (CTCL).FEBS letters · 2021Article
- Phloretin Alleviates Arsenic Trioxide-Induced Apoptosis of H9c2 Cardiomyoblasts via Downregulation in CaCardiovascular toxicology · 2021Article
- Myonectin inhibits adipogenesis in 3T3-L1 preadipocytes by regulating p38 MAPK pathway.BMB reports · 2021Article
- p38β and Cancer: The Beginning of the Road.International journal of molecular sciences · 2020Review
24 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Nuclear factor of activated T cells (NFAT) is implicated in multiple biological processes, including cytokine gene expression, cardiac hypertrophy, and adipocyte differentiation. A conserved NFAT homology domain is identified in all NFAT members. Dephosphorylation of the NFAT homology region is critical for NFAT nuclear translocation and transcriptional activation. Here we demonstrate that NFATc4 is phosphorylated by p38 mitogen-activated protein (MAP) kinase but not by JNK. The p38 MAP kinase phosphorylates multiple residues, including Ser(168) and Ser(170), in the NFAT homology domain of NFATc4. Replacement of Ser(168,170) with Ala promotes nuclear localization of NFATc4 and increases NFAT-mediated transcription activity. Stable expression of Ala(168,170) NFATc4, but not of wild-type NFATc4, in NIH 3T3 cells promotes adipocyte formation under differentiation conditions. Molecular analysis indicates that peroxisome proliferator-activated receptor gamma 2 (PPAR gamma 2) is a target of NFAT. Two distinct NFAT binding elements are located in the PPAR gamma 2 gene promoter. Stable expression of Ala(168,170) NFATc4, but not of wild-type NFATc4, increases the expression of PPAR gamma, which contributes in part to increased adipocyte formation. Thus, NFAT regulates PPAR gamma gene expression and has a direct role in adipocyte differentiation.
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Registered trials
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