Transcriptional activation and transformation by FosB protein require phosphorylation of the carboxyl-terminal activation domain.
Transcriptional activation and transformation by FosB protein require phosphorylation of the carboxyl-terminal activation domain.
复制标题
FosB 蛋白的转录激活和转化需要羧基末端激活结构域的磷酸化。
DOI：
10.1128/mcb.17.5.2372
复制
发表时间：
1997
影响因子：
5.3
通讯作者：
Wisdom,R
中科院分区：
文献类型：
--
作者：
Skinner,M;Qu,S;Moore,C;Wisdom,R
The transcription factor AP-1, composed of Fos-Jun dimers, mediates some aspects of the cellular response to growth factors. Transcriptional activation and neoplastic transformation by FosB, a member of the Fos family of proteins, require the presence of a potent C-terminal activation domain. Here we show by mutational analysis that the FosB C-terminal domain has a proline-based motif that is essential for both of these functions. Phosphopeptide mapping experiments show that the C terminus of FosB is phosphorylated within a cluster of functionally redundant serine residues that is adjacent to this proline-based motif. Mutation of these serine residues to alanine severely reduces the ability of this region to function as an activation domain and inhibits the ability of FosB protein to function as a transforming protein. Several observations suggest that the kinase responsible for phosphorylation of these sites is distinct from the mitogen-activation protein kinases and stress-activated protein kinases. Our results show that transcriptional activation and neoplastic transformation by the FosB protein are dependent on phosphorylation within the C terminus. This form of control may provide a potential mechanism of signal integration at the level of a single transcription factor.
