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Journal of Cell Science 115, e2005-e2005 (2002)
Copyright © 2002 The Company of Biologists Limited
doi:


In this issue

NF-{kappa}B: a novel target for ß3-endonexin

ß3-endonexin is an integrin-binding protein that binds specifically to the cytoplasmic tail of integrin ß3. The protein is thought to participate in integrin recycling but might also regulate cell cycle progression, since it can bind to cyclin A and inhibit the activity of cyclin-dependent kinase 2 (CDK2). Meinrad Gawaz and co-workers now show that ß3-endonexin can also interact with another important cellular regulator: the transcription factor NF-{kappa}B (see p. 3879). They demonstrate that integrin-ß3-dependent repression of the urokinase-type plasminogen receptor (uPAR) gene can be mimicked by overexpression of ß3-endonexin and that this requires the NF-{kappa}B-binding site in the uPAR promoter. The authors also find that ß3-endonexin splice forms contain a KRKK sequence that allows them to translocate to the nucleus. Furthermore, they show that ß3-endonexin physically associates with the p50-p65 NF-{kappa}B complex in vivo and can interfere with its binding to oligonucleotides containing the NF-{kappa}B consensus sequence. These findings thus not only reveal a nuclear role for this integrin-associated protein but also provide evidence for a novel adhesion-dependent mechanism for NF-{kappa}B regulation.


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Related articles in JCS:

Role of ß3-endonexin in the regulation of NF-{kappa}B-dependent expression of urokinase-type plasminogen activator receptor
Felicitas Besta, Steffen Massberg, Korbinian Brand, Elke Müller, Sharon Page, Sabine Grüner, Michael Lorenz, Karin Sadoul, Waldemar Kolanus, Ernst Lengyel, and Meinrad Gawaz
JCS 2002 115: 3879-3888. [Abstract] [Full Text]  




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