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Nfatc4

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Nfatc4

Nuclear factor of activated T-cells, cytoplasmic, calcineurin-dependent 4
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols  ; NF-AT3; NF-ATC4; NFAT3
External IDs GeneCards:
RNA expression pattern
Orthologs
Species Human Mouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)
RefSeq (protein)
Location (UCSC)
PubMed search

Nuclear factor of activated T-cells, cytoplasmic 4 is a protein that in humans is encoded by the NFATC4 gene.[1][2]

Function

The product of this gene is a member of the nuclear factors of activated T cells DNA-binding transcription complex. This complex consists of at least two components: a preexisting cytosolic component that translocates to the nucleus upon T cell receptor (TCR) stimulation and an inducible nuclear component. Other members of this family of nuclear factors of activated T cells also participate in the formation of this complex. The product of this gene plays a role in the inducible expression of cytokine genes in T cells, especially in the induction of the IL-2 and IL-4.[2]

NFAT transcription factors are implicated in breast cancer, more specifically in the process of cell motility at the basis of metastasis formation. Indeed NFAT3 (NFATc4) is an inhibitor of cell motility by blocking the expression of LCN2.[3]

Interactions

NFATC4 has been shown to interact with CREB-binding protein.[4]

See also

References

  1. ^ Hoey T, Sun YL, Williamson K, Xu X (Jun 1995). "Isolation of two new members of the NF-AT gene family and functional characterization of the NF-AT proteins". Immunity 2 (5): 461–72.  
  2. ^ a b "Entrez Gene: NFATC4 nuclear factor of activated T-cells, cytoplasmic, calcineurin-dependent 4". 
  3. ^ Fougère M, Gaudineau B, Barbier J, Guaddachi F, Feugeas JP, Auboeuf D, Jauliac S (April 2010). "NFAT3 transcription factor inhibits breast cancer cell motility by targeting the Lipocalin 2 gene". Oncogene 29 (15): 2292–301.  
  4. ^ Yang T, Davis RJ, Chow CW (October 2001). "Requirement of two NFATc4 transactivation domains for CBP potentiation". J. Biol. Chem. 276 (43): 39569–76.  


Further reading

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This article incorporates text from the United States National Library of Medicine, which is in the public domain.

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