Distinct effects of cAMP and mitogenic signals on CREB-binding protein recruitment impart specficity to target gene activation via CREB

被引:154
|
作者
Mayr, BM [1 ]
Canettieri, G [1 ]
Montminy, MR [1 ]
机构
[1] Salk Inst Biol Studies, Peptide Biol Labs, La Jolla, CA 92037 USA
关键词
D O I
10.1073/pnas.191152098
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
Ser-133 phosphorylation of the cAMP-responsive element-binding protein (CREB) is sufficient to induce cellular gene expression in response to cAMP, but additional promoter-bound factors are required for target gene activation by CREB in response to nitogen/stress signals. To compare the relative effects of different signals on recruitment of the coactivator CREB-binding protein (CBP) to CREB in living cells, we developed a fluorescence resonance energy transfer (FRET) assay. cAMP promoted the interaction of CREB with CBP in a phosphorylation-dependent manner by FRET analysis, but nitogen/stress signals were far less effective in stimulating complex formation even though they induced comparable levels of Ser-133 phosphorylation. cAMP and non-cAMP stimuli were comparably active in promoting this interaction in the cytosol; the formation of CREB-CBP complexes in response to non-cAMP signals was specifically inhibited in the nucleus. Non-cAMP signals had no effect on intrinsic CREB- or CBP-binding activities by Far Western blot assay, thereby supporting the presence of a distinct CREB-CBP antagonist. Our studies indicate that the relative effects of cAMP and nitogen/stress signals on CREB-CBP complex formation impart selectivity to gene activation through CREB phosphorylated at Ser-133.
引用
收藏
页码:10936 / 10941
页数:6
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