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First published online August 24, 2006

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NF-B - capped by 14-3-3

The transcription factor NF-B has important roles in the immune response, cancer and inflammation. Its inhibitors, IB proteins, generally anchor NF-B in the cytoplasm until an activation signal from a ligand such as tumour necrosis factor (TNF) is received. IB, however, actively removes NF-B from the nucleus in unstimulated cells or when signalling must be terminated. On p. 3695, Lluís Espinosa and co-workers implicate another important signalling mechanism - 14-3-3 proteins - in this process. 14-3-3 proteins control the activity, localization and stability of various signalling molecules. Espinosa and co-workers now demonstrate that 14-3-3 proteins interact with both p65 NF-B and IB. They identify the binding sites involved and show that mutations in these cause p65 NF-B and IB to remain in the nucleus. The authors go on to show that TNF promotes recruitment of 14-3-3 proteins to NF-B-dependent promoters and that dominant negative 14-3-3 constructs compromise the responses of these promoters to TNF. 14-3-3 proteins thus appear to be critical for nuclear export of NF-B, re-establishing the basal level conditions that allow it to be rapidly activated by stimuli such as TNF.

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Related articles in JCS:

Efficient nuclear export of p65-IB complexes requires 14-3-3 proteins

Cristina Aguilera, Vanessa Fernández-Majada, Julia Inglés-Esteve, Verónica Rodilla, Anna Bigas, and Lluís Espinosa
JCS 2006 119: 3695-3704. [Abstract] [Full Text]  

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Related articles in JCS Similar articles in this journal Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via Google Scholar Google Scholar Search for Related Content Social Bookmarking                         What's this?