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A Switch in Distinct IB Degradation Mechanisms Mediates Constitutive NF-B Activation in Mature B Cells¹

Erika R. Fields^*, Bradley J. Seufzer^*, Eugene M. Oltz and Shigeki Miyamoto^2,*

^* Department of Pharmacology, University of Wisconsin Medical School, Madison, WI 53792; and Department of Microbiology and Immunology, Vanderbilt University School of Medicine, Nashville, TN 37232

Inducible activation of cytoplasmic NF-B/Rel transcription factors occurs via proteasome-dependent degradation of an associated inhibitor, termed IB. Mature B lymphocytes constitutively express nuclear NF-B, which is important for their long-term survival. The intrinsic mechanisms by which B cells constitutively activate NF-B are unknown. In this paper we demonstrate that maintenance of NF-B activity in primary B cells is mediated by a novel calcium-dependent, but proteasome-independent, mechanism. Moreover, we show that differentiation of conditionally transformed pre-B cells is accompanied by a switch from proteasome-dependent to proteasome-independent degradation of IB. Our findings indicate that IB degradation mechanisms are dynamic during B cell development, and ultimately establish constitutive NF-B activity in mature B lymphocytes.

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