A transcriptively active complex of APP with Fe65 and histone acetyltransferase Tip60
A transcriptively active complex of APP with Fe65 and histone acetyltransferase Tip60
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DOI：
10.1126/science.1058783
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发表时间：
2001-07-06
期刊：
影响因子：
56.9
通讯作者：
Südhof, TC
中科院分区：
文献类型：
--
作者：
Cao, XW;Südhof, TC
淀粉样β前体蛋白（APP）是一种广泛表达的细胞表面蛋白。在跨膜区被γ-分泌酶裂解，APP的γ-裂解产生阿尔茨海默病的细胞外淀粉样β-肽，并释放出生理功能未知的细胞内尾片段。我们现在证明，APP的胞质尾形成一个多聚体的复合物与核衔接蛋白Fe 65和组蛋白乙酰转移酶Tip 60。该复合物通过异源Gal 4-或LexA-DNA结合结构域有效地刺激转录，表明通过γ-切割释放APP的胞质尾可能在基因表达中起作用。
Amyloid-beta precursor protein (APP) a widely expressed cell-surface protein. is cleaved in the transmembrane region by gamma -secretase, gamma -Cleavage Of APP produces the extracellular amyloid beta -peptide of Alzheimer's disease and releases an intracellular tail fragment of unknown physiological function. We now demonstrate that the cytoplasmic tail of APP forms a multimeric complex with the nuclear adaptor protein Fe65 and the histone acetyltransferase Tip60. This complex potently stimulates transcription via heterologous Gal4- or LexA-DNA binding domains, suggesting that release of the cytoplasmic tail of APP by gamma -cleavage may function in gene expression.