Journal
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Volume 389, Issue 2, Pages 205-210Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bbrc.2009.08.074
Keywords
Ubiquitin; Processing; NF-kappa B; p105; p50; ABIN-1
Categories
Funding
- Sheldon Adelson Foundation for Medical Research (AIVIRF)
- Israel Science Foundation (ISF)
- German-Israeli Foundation for Research and Scientific Development (GIF)
- European Union (EU)
- Networks of Excellence (NeOEs)
- Israel Cancer Research Fund (ICRF) USA
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p105 plays dual roles in NF-kappa B signaling: in its precursor form it inhibits NF-kappa B activation, but limited processing by the ubiquitin system generates the p50 active subunit of the transcription factor. Here we show that ABIN-1, an A20-binding protein that is also known to attenuate NF-kappa B activation, inhibits p105 processing. p105 and ABIN-1 physically interact with one another, but the binding is not necessary for inhibition of processing. Rather, it appears to stabilize ABIN-1 and to increase its level, which further augments its inhibitory effect. Deletion of the processing inhibitory domain (PID) of p105 abrogates the inhibition which also requires the ABIN homology domain (AHD)-2 of ABIN-1. Together, the effects of ABIN-I on p105 processing and of p105 on stabilizing ABIN-1 act to potentiate the NF-kappa B inhibitory activity of ABIN-1. (C) 2009 Elsevier Inc. All rights reserved.
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