Cyclin Y 是在 eumetazoans 之中的高度保存的 cyclin,然而,它的功能和规定糟糕被理解。到 searchfor Cyclin 交往 Y 蛋白质,我们屏蔽了酵母把人的 Cyclin Y (CCNY ) 用作一个诱饵和 identifiedthe 追随者 interactors 的二混血儿的图书馆:CDK14 和 14-3-3 家庭的四个成员(,,,) 。在 CCNY 和 14-3-3proteins 之间的相互作用在 vitro 并且在 vivo 被证实。结果证明在 CCNY 的 Ser-100 和 Ser-326 残余为 14-3-3 绑定是关键的。有趣地,到 14-3-3 的有约束力的 ofCCNY 显著地提高了在 CCNY 和 CDK14 之间的协会。我们的调查结果可以增加对它的 kinase 搭挡有约束力的 regulationof CCNY 的新层。
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 (ε,β,η,τ). 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.