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B
1
Departments of
*
Laboratory Medicine and Pathology,
Medicine, and
Biochemistry, Boston University Medical School, Boston, MA 02118
Rapid I
B
turnover has been implicated in the high basal
NF-B activity in WEHI 231 B immature IgM+ B cells. Here
we show that treatment of WEHI 231 cells with apigenin, a selective
inhibitor of the protein kinase CK2, decreased the rate of IB
turnover and nuclear levels of NF-B. Turnover of IB in these
cells is mediated in part by the protease calpain. Since both CK2 and
calpain target the proline-glutamic acid-serine-threonine (PEST)
domain, we investigated the role of CK2 in the degradation of IB
by calpain using an in vitro phosphorylation/degradation assay. CK2
phosphorylation enhanced µ-calpain-mediated degradation of wild-type
IB, but not of mutant 3CIB, with S283A, T291A, and T299A
mutations in phosphorylation sites within the PEST domain. Roles for
CK2 and calpain in IB turnover were similarly shown in CH31
immature and CH12 mature IgM+ B cells, but not in A20 and
M12 IgG+ B cells. These findings demonstrate for the first
time that CK2 phosphorylation of serine/threonine residues in the PEST
domain promotes calpain-mediated degradation of IB and thereby
increases basal NF-B levels in IgM+ B
cells.
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