期刊
MOLECULAR AND CELLULAR BIOLOGY
卷 21, 期 14, 页码 4837-4846出版社
AMER SOC MICROBIOLOGY
DOI: 10.1128/MCB.21.14.4837-4846.2001
关键词
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资金
- NIAID NIH HHS [AI-41035, R01 AI041035, R21 AI041035] Funding Source: Medline
Mature B lymphocytes are unique in containing nuclear Rel proteins prior to cell stimulation. This activity consists largely of p50-c-Rel heterodimers, and its importance for B-cell function is exemplified by reduced B-cell viability in several genetically altered mouse strains. Here we suggest a mechanism for the cell specificity and the subunit composition of constitutive B-cell NF-KB based on the observed properties of Rel homo- and heterodimers and I kappaB alpha. We show that c-Rel lacks a nuclear export sequence, making the removal of c-Rel-containing complexes from the nucleus less efficient than removal of p65-containing complexes. Second, the nuclear import potential of p65 and c-Rel homodimers but not p50-associated heterodimers was attenuated when they were complexed to I kappaB alpha, leading to a greater propensity of heterodimers to be nuclear. We propose that subunit composition of B-cell NF-KB reflects the inefficient retrieval of p50-c-Rel heterodimers from the nucleus. Cell specificity may be a consequence of c-Rel-I kappaB alpha complexes being present only in mature B cells, which leads to nuclear c-Rel due to I kappaB alpha turnover and shuttling of the complex.
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