Modification by nuclear export?
Article Abstract:
Research into the regulated nuclear export of NF-AT4, a transcription factor with both a nuclear-localization signal and a nuclear-export signal, indicates that the phosphatase calcineurin antagonizes the export receptor Crm1-mediated nuclear export of NF-AT4. Calcineurin was found to compete with Crm1 for binding to NF-AT4. It appears that Crm1-mediated export, and the competition between Crm1 and calcineurin, affect whether or not nuclear NF-AT4 is incorporated into a productive transcriptional complex.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1999
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Structure of the DNA-binding domains from NFAT, Fos and Jun bound specifically to DNA
Article Abstract:
The three dimensional structure of the site where the nuclear factor of activated T-cells (NFAT) and AP-1 heterodimer (Fos-Jun) bind to DNA has been studied using crystallography, and shows a groove in the structure where 15 base pairs can be recognised. The overall complex shows tight binding but is likely to be a substructure of a larger structure, and could have additional components associated with it. The MOLSCRIPT program was used to generate the three dimensional representations.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1998
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