期刊
MOLECULAR AND CELLULAR BIOLOGY
卷 20, 期 6, 页码 2269-2284出版社
AMER SOC MICROBIOLOGY
DOI: 10.1128/MCB.20.6.2269-2284.2000
关键词
-
资金
- NIAID NIH HHS [AI 41035, R21 AI041035, R01 AI041035] Funding Source: Medline
- NIGMS NIH HHS [GM54768] Funding Source: Medline
- NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES [R21AI041035, R01AI041035] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM054768] Funding Source: NIH RePORTER
Rel and I kappa B protein families form a complex cellular regulatory network A major regulatory function of I kappa B proteins is to retain Rel proteins in the cell cytoplasm. In addition, I kappa B proteins have also been postulated to serve nuclear functions. These include the maintenance of inducible NF-kappa B-dependent gene transcription, as well as termination of inducible transcription. We show that I kappa B alpha shuttles between the nucleus and the cytoplasm, utilizing the nuclear export receptor CRM1, A CRM1-binding export sequence was identified in the N-terminal domain of I kappa B alpha but not in that of I kappa B beta or I kappa B epsilon. By reconstituting major aspects of NF-kappa B-I kappa B sequestration in yeast, we demonstrate that cytoplasmic retention of p65 (also called ReIA) by I kappa B alpha requires Crm1p-dependent nuclear export. In mammalian cells, inhibition of CRM1 by leptomycin B resulted in nuclear localization of cotransfected p65 and I kappa B alpha in COS cells and enhanced nuclear relocation of endogenous p65 in T cells. These observations suggest that the main function of I kappa B alpha is that of a nuclear export chaperone rather than a cytoplasmic tether. We propose that the nucleus is the major site of p65-I kappa B alpha association, from where these complexes must be exported in order to create the cytoplasmic pool.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据