期刊
MOLECULAR CELL
卷 22, 期 2, 页码 231-243出版社
CELL PRESS
DOI: 10.1016/j.molcel.2006.03.010
关键词
-
资金
- Wellcome Trust Funding Source: Medline
SATB1 regulates gene expression by acting as a docking site for several chromatin remodeling enzymes and also by recruiting corepressors; (HDACs) or coactivators (HATs) directly to promoters. However, how these contrasting effectors act at the level of SATB1 is not clear. We show here that phosphorylation by PKC acts as a switch to determine whether SATB1 interacts with HDAC1 or PCAF. Phosphorylation and dephosphorylation of SATB1 exerted opposing effects on MAR-linked reporter activity in vivo. SATB1 interacted with both CBP/p300 and PCAF HATs; however, these interactions resulted in the acetylation of the PDZ-Iike domain of SATB1 by PCAF but not by CBP/p300 and resulted in loss of its DNA binding activity. Using the T cell activation model, we provide mechanistic insights into how IL-2 transcription is reciprocally governed by the phosphorylation status of SATB1 and propose that a similar mechanism may dictate the ability of SATB1 to function as a global regulator.
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