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Identification of Pygopus-2’ s Interacting Proteins by Tandem Affinity Purification

Abstract

摘要 Pygopus2(Pygo2)是2002年发现的,为Wnt信号通路中ß-catenin的下游功能蛋白。Pygo2有两个独特的保守结构域,即N端的NHD结构域和C端的锌指结构模体PHD。已有研究证明,Pygo2的PHD结构域可通过Lgs/BCL9与ß-catenin结合。而NHD结构域则被认为在无PHD存在下可激活Wnt靶蛋白的转录。从整个蛋白上看,PHD与Lgs/BCL9的结合可增强基因的转录,通过以下两种方式:1)把NHD带至β-catenin/LEF转录复合体或靶基因上,推动转录的进行。2)把ß-catenin锚定在核内,以提高β-catenin...Abstract Pygopus2 (Pygo2) was first found in 2002 as a functional protein in Wnt signaling pathway and dowmstream partner of ß-catenin. Pygo2 protein have two distinct conserved domains, an N-terminal homology domain (NHD) and a C-terminal PHD zinc finger motif. Pygo binds to the N-terminal domain of β-catenin via Lgs/BCL9 through its PHD domain. The NHD motif can activate Wnt target genes ...学位:理学硕士院系专业:生命科学学院生物医学科学系_生物化学与分子生物学学号:2012005130212

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