Cyclin Y, a novel membrane-associated cyclin, interacts with PFTK1
Cyclin Y, a novel membrane-associated cyclin, interacts with PFTK1
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Cyclin Y 是一种新型膜相关细胞周期蛋白，与 PFTK1 相互作用
DOI：
10.1016/j.febslet.2009.06.010
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发表时间：
2009-07-07
期刊：
影响因子：
3.5
通讯作者：
Chen, Jiangye
中科院分区：
文献类型：
--
作者：
Jiang, Mei;Gao, Yankun;Chen, Jiangye
在酵母双杂交筛选中，一个新的细胞周期蛋白CCNY被鉴定为PFTK1相互作用蛋白。CCNY中的Cyclin box和PFTK1中的PFTAIRE基序都是相互作用所必需的，体内外实验都证实了这一点。Northern印迹分析检测到CCNY的两个转录本(4 kb和2 kb)，并且由于N-末端的肉豆蔻酰化信号，CCNY在质膜上富含。结构概要：MINT-7147585，MINT-7147598，MINT-7147614，MINT-7147628，MINT-7147647，MINT-7147665，MINT7147680：PFTK1(unprotkb：O94921)通过两个杂交分子(MI：0018)与CCNY(uniprotkb：Q8ND76)物理作用，MINT-7147743：pftk1(uniprotkb：O94921)与CCNY(uniprotkb：Q8ND76)通过反标记免疫共沉淀(MI：0007)和CCNY(uniprotkb：O35495)通过反诱饵免疫共沉淀(MI：0006)mint-7147695：pftk1(uniprotkb：Q8BGU5)物理结合(MI：0403)。荧光显微镜(MI：0416)(C)2009年欧洲生化学会联合会。爱思唯尔出版公司版权所有。
A novel cyclin, CCNY, was identified as a PFTK1 interacting protein in a yeast two-hybrid screen. The cyclin box in CCNY and the PFTAIRE motif in PFTK1 are both required for the interaction which was confirmed by in vivo and in vitro assays. Two transcripts (4 and 2 kb), of CCNY were detected by Northern blot analysis and CCNY was enriched at the plasma membrane due to an N-terminal myristoylation signal. We propose that binding of CCNY to PFTK1 enhances PFTK1 kinase activity and changes its intracellular location.Structured summary:MINT-7147585, MINT-7147598, MINT-7147614, MINT-7147628, MINT-7147647, MINT-7147665, MINT7147680: pftk1 (uniprotkb: O94921) physically interacts (MI: 0915) with CCNY (uniprotkb: Q8ND76) by two hybrid (MI: 0018)MINT-7147725, MINT-7147743: pftk1 (uniprotkb: O94921) physically interacts (MI: 0914) with CCNY (uniprotkb: Q8ND76) by anti tag coimmunoprecipitation (MI: 0007)MINT-7147758: pftk1 (uniprotkb: O35495) physically interacts (MI: 0914) with CCNY (uniprotkb: Q8BGU5) by anti bait coimmunoprecipitation (MI: 0006)MINT-7147695, MINT-7147713: pftk1 (uniprotkb: O94921) and CCNY (uniprotkb: Q8ND76) colocalize (MI: 0403) by. uorescence microscopy (MI: 0416) (C) 2009 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.