Protein-protein interactions in the yeast pheromone response pathway: Ste5p interacts with all members of the MAP kinase cascade.

Protein-protein interactions in the yeast pheromone response pathway: Ste5p interacts with all members of the MAP kinase cascade.
复制标题

酵母信息素响应途径中的蛋白质-蛋白质相互作用:Ste5p 与 MAP 激酶级联的所有成员相互作用。

DOI:
10.1093/genetics/138.3.609
复制
发表时间:
1994
期刊:
影响因子:
3.3
通讯作者:
SpragueJr,GF
SpragueJr,GF
中科院分区:
生物学2区
文献类型:
--
作者:
Printen,JA;SpragueJr,GF

文献摘要

被引文献

相似文献

我们已经使用Fields和Song的双杂交系统来鉴定发生在酿酒酵母信息素反应途径中的蛋白质-蛋白质相互作用。在所有配对组合中测试了途径成分Ste4p、Ste5p、Ste7p、Ste11p、Ste12p、Ste20p、Fus3p和Kss 1p。我们检测到的所有相互作用都至少涉及作为反应途径中心元件的MAP激酶级联中的一个成员。Ste5p是一种生化功能未知的蛋白质,它与MAP激酶级联反应的每个步骤中的蛋白激酶相互作用,特别是与Ste11p(一种MEKK)、Ste7p(一种MEK)和Fus3p(一种MAP激酶)。这一发现表明,Ste5p的一个作用是作为支架,促进激酶级联成员之间的相互作用。作为促进者,Ste5p可以使信号传播和信号衰减都更有效。步骤5p也可能有助于减少与其他MAP激酶级联的串扰,从而确保信息素反应途径的完整性。我们还发现Ste11p和Ste7p都与Fus3p和Kss1p相互作用。最后,我们检测到其中一个MAP激酶Kss 1p与一个假定的靶点Ste12p之间的相互作用。我们未能检测到Ste4p或Ste20p与反应途径的任何其他组件的相互作用。
We have used the two-hybrid system of Fields and Song to identify protein-protein interactions that occur in the pheromone response pathway of the yeast Saccharomyces cerevisiae. Pathway components Ste4p, Ste5p, Ste7p, Ste11p, Ste12p, Ste20p, Fus3p and Kss1p were tested in all pairwise combinations. All of the interactions we detected involved at least one member of the MAP kinase cascade that is a central element of the response pathway. Ste5p, a protein of unknown biochemical function, interacted with protein kinases that operate at each step of the MAP kinase cascade, specifically with Ste11p (an MEKK), Ste7p (an MEK), and Fus3p (a MAP kinase). This finding suggests that one role of Ste5p is to serve as a scaffold to facilitate interactions among members of the kinase cascade. In this role as facilitator, Ste5p may make both signal propagation and signal attenuation more efficient. Ste5p may also help minimize cross-talk with other MAP kinase cascades and thus ensure the integrity of the pheromone response pathway. We also found that both Ste11p and Ste7p interact with Fus3p and Kss1p. Finally, we detected an interaction between one of the MAP kinases, Kss1p, and a presumptive target, the transcription factor Ste12p. We failed to detect interactions of Ste4p or Ste20p with any other component of the response pathway.