14-3-3 Binding to Cyclin Y contributes to cyclin Y/CDK14 association
文献类型:期刊论文
作者 | Li, S; Jiang, M; Wang, WJ; Chen, JY |
刊名 | ACTA BIOCHIMICA ET BIOPHYSICA SINICA
![]() |
出版日期 | 2014 |
卷号 | 46期号:4页码:299-304 |
关键词 | cyclin Y 14-3-3 protein 14-3-3 binding motif |
通讯作者 | Chen, JY (reprint author), Chinese Acad Sci, Shanghai Inst Biol Sci, Inst Biochem & Cell Biol, Shanghai 200031, Peoples R China.,jychen@sibcb.ac.cn |
英文摘要 | Cyclin Y is a highly conserved cyclin among eumetazoans, yet its function and regulation are poorly understood. To search for Cyclin Y-interacting proteins, we screened a yeast two-hybrid library using human Cyclin Y (CCNY) as a bait and identified the following interactors: CDK14 and four members of the 14-3-3 family (epsilon, beta, eta, tau). The interaction between CCNY and 14-3-3 proteins was confirmed both in vitro and in vivo. The results showed that Ser-100 and Ser-326 residues in CCNY were crucial for 14-3-3 binding. Interestingly, binding of CCNY to 14-3-3 significantly enhanced the association between CCNY and CDK14. Our findings may add a new layer of regulation of CCNY binding to its kinase partner. |
学科主题 | Biochemistry & Molecular Biology; Biophysics |
类目[WOS] | Biochemistry & Molecular Biology ; Biophysics |
关键词[WOS] | CONSERVED CYCLIN ; IN-VIVO ; PROTEINS ; KINASE ; 14-3-3-PROTEINS ; PHOSPHORYLATION ; ACTIVATION ; DOMAINS ; CRK1 ; FORM |
收录类别 | SCI |
语种 | 英语 |
WOS记录号 | WOS:000334023100006 |
版本 | 出版稿 |
源URL | [http://202.127.25.143/handle/331003/178] ![]() |
专题 | 上海生化细胞研究所_上海生科院生化细胞研究所 |
推荐引用方式 GB/T 7714 | Li, S,Jiang, M,Wang, WJ,et al. 14-3-3 Binding to Cyclin Y contributes to cyclin Y/CDK14 association[J]. ACTA BIOCHIMICA ET BIOPHYSICA SINICA,2014,46(4):299-304. |
APA | Li, S,Jiang, M,Wang, WJ,&Chen, JY.(2014).14-3-3 Binding to Cyclin Y contributes to cyclin Y/CDK14 association.ACTA BIOCHIMICA ET BIOPHYSICA SINICA,46(4),299-304. |
MLA | Li, S,et al."14-3-3 Binding to Cyclin Y contributes to cyclin Y/CDK14 association".ACTA BIOCHIMICA ET BIOPHYSICA SINICA 46.4(2014):299-304. |
入库方式: OAI收割
浏览0
下载0
收藏0
其他版本
除非特别说明,本系统中所有内容都受版权保护,并保留所有权利。