التفاصيل البيبلوغرافية
| العنوان: |
Regulation of NF-κB activity and inducible nitric oxide synthase by regulatory particle non-ATPase subunit 13 (Rpn13). |
| المؤلفون: |
Mazumdar, Tuhina1 teissa@bcm.tmc.edu, Gorgun, Murat F.1, Youbao Sha1, Tyryshkin, Alexey1, Shenyan Zeng1, Hartmann-Petersen, Rasmus2, J&3x00F8;rgensen, Jakob Ploug2, Hendil, Klavs B.2, Eissa, Tony N.1 |
| المصدر: |
Proceedings of the National Academy of Sciences of the United States of America. 8/3/2010, Vol. 107 Issue 31, p13854-13859. 6p. |
| مصطلحات موضوعية: |
*NITRIC oxide, *CELL adhesion molecules, *ADENOSINE triphosphatase, *INFLAMMATION, *CELL proliferation, *PROTEINS |
| مستخلص: |
Human Rpn13, also known as adhesion regulating molecule 1 (ADRM1), was recently identified as a novel 19S proteasome capassociated protein, which recruits the deubiquitinating enzyme UCH37 to the 265 proteasome. Knockdown of Rpn13 by 5iRNA does not lead to global accumulation of ubiquitinated cellular proteins or changes in proteasome expression, suggesting that Rpnl3 must have a specialized role in proteasome function. Thus, Rpn13 participation in protein degradation, by recruiting UCH37, is rather selective to specific proteins whose degradation critically depends on UCH37 deubiquitination activity. The specific substrates for the Rpn13/UCH37 complex have not been determined. Because of a previous discovery of an interaction between Rpn13 and inducible nitric oxide synthase (iNOS), we hypothesized that iNOS is one of the substrates for the Rpn13/UCH37 complex. In this study, we show that Rpn13 is involved in iNOS degradation and is required for iNOS interaction with the deubiquitination protein LJCH37. Furthermore, we discovered that lxB-a, a protein whose proteasomal degradation activates the transcription factor NF-κB, is also a substrate for the Rpn13/UCH37 complex. Thus, this study defines two substrates, with important roles in inflammation and host defense for the Rpn13/UCH37 pathway. [ABSTRACT FROM AUTHOR] |
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