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Phosphorylation of CREB at Ser-133 induces complex formation with CREB-binding protein via a direct mechanism. 总被引:20,自引:10,他引:10 下载免费PDF全文
D Parker K Ferreri T Nakajima V J LaMorte R Evans S C Koerber C Hoeger M R Montminy 《Molecular and cellular biology》1996,16(2):694-703
We have characterized a phosphoserine binding domain in the coactivator CREB-binding protein (CBP) which interacts with the protein kinase A-phosphorylated, and hence activated, form of the cyclic AMP-responsive factor CREB. The CREB binding domain, referred to as KIX, is alpha helical and binds to an unstructured kinase-inducible domain in CREB following phosphorylation of CREB at Ser-133. Phospho-Ser-133 forms direct contacts with residues in KIX, and these contacts are further stabilized by hydrophobic residues in the kinase-inducible domain which flank phospho-Ser-133. Like the src homology 2 (SH2) domains which bind phosphotyrosine-containing peptides, phosphoserine 133 appears to coordinate with a single arginine residue (Arg-600) in KIX which is conserved in the CBP-related protein P300. Since mutagenesis of Arg-600 to Gln severely reduces CREB-CBP complex formation, our results demonstrate that, as in the case of tyrosine kinase pathways, signal transduction through serine/threonine kinase pathways may also require protein interaction motifs which are capable of recognizing phosphorylated amino acids. 相似文献
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Magnitude of the CREB-dependent transcriptional response is determined by the strength of the interaction between the kinase-inducible domain of CREB and the KIX domain of CREB-binding protein 总被引:7,自引:0,他引:7 下载免费PDF全文
Shaywitz AJ Dove SL Kornhauser JM Hochschild A Greenberg ME 《Molecular and cellular biology》2000,20(24):9409-9422
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What turns CREB on? 总被引:20,自引:0,他引:20
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