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Phosphorylation of the Spi‐B transcription factor reduces its intrinsic stability
Author(s) -
Ray-Gallet Dominique,
Moreau-Gachelin Françoise
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)01687-7
Subject(s) - phosphorylation , serine , transcription factor , chemistry , microbiology and biotechnology , transcription (linguistics) , iκb kinase , casein kinase 2 , iκbα , biochemistry , gene , protein kinase a , biology , signal transduction , nf κb , cyclin dependent kinase 2 , linguistics , philosophy
The Spi‐B transcription factor is an Ets protein expressed in B lymphoid cells and closely related to the Spi‐1/PU.1 oncoprotein. By mutational analysis, we showed that Spi‐B is phosphorylated by casein kinase II in vitro on four serine residues. Mutation of these four serines to alanines prevented the phosphorylation of Spi‐B in vivo, increased the ability of Spi‐B to transactivate expression of a reporter gene and led to a decrease of Spi‐B stability. We propose that the phosphorylation of Spi‐B may participate in the modulation of Spi‐B functional activity by controlling its intracellular protein level.