Nore1B regulates TCR signaling via Ras and Carma1

Cellular Signalling
Kazuhiro IshiguroRamnik Xavier

Abstract

Nore1A was originally identified as a potential Ras effector, and Nore1B is an alternatively spliced isoform. Both share a Ras/Rap association domain (RA domain) but only Nore1A contains sequence motifs that predict SH3 domain binding and diacylglycerol/phorbol ester binding in the amino-terminal region. Here we report that Carma1 binds to Nore1A and Nore1B through the RA domain and that Carma1 interacts with active Ras in the presence of Nore1B. RNA interference against Nore1B attenuates NF-kappaB activation induced by T cell receptor (TCR) ligation, but not NF-kappaB activation induced by TNFalpha or lipoteichoic acid. In addition, Nore1B is also required for KiRas GV12-mediated ERK1 activation and Elk1 reporter activity in T cells. We also provide evidence that knockdown of Nore1B also impairs polarized redistribution of Ras at the B cell-T cell immune interface. Together, these findings suggest that endogenous Nore1B recruits active Ras to the APC-T cell interface and mediates the interaction between Ras and Carma1.

References

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Citations

Jul 14, 2007·Cellular and Molecular Life Sciences : CMLS·J OmerovicI A Prior
Dec 19, 2008·The Journal of Biological Chemistry·Joseph AvruchFan Xia
Sep 2, 2008·American Journal of Respiratory Cell and Molecular Biology·Benjamin D MedoffRamnik J Xavier
Mar 13, 2014·FEBS Letters·Natalia VolodkoShairaz Baksh
Jan 9, 2009·European Journal of Immunology·Benjamin D MedoffRamnik J Xavier
Apr 7, 2009·Biochimica Et Biophysica Acta·Antje M RichterReinhard H Dammann
Aug 19, 2007·Biochimica Et Biophysica Acta·Louise van der Weyden, David J Adams
Dec 14, 2019·Genes & Diseases·Mohammad Reza ZinatizadehSeyed Rouhollah Miri

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