...
  • 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Molecular and Cellular Biology >Spa2p Interacts with Cell Polarity Proteins and Signaling Components Involved in Yeast Cell Morphogenesis
【24h】

Spa2p Interacts with Cell Polarity Proteins and Signaling Components Involved in Yeast Cell Morphogenesis

机译：Spa2p与细胞极性蛋白和参与酵母细胞形态发生的信号转导成分相互作用。

获取原文
           
页面导航
  • 摘要
  • 著录项
  • 相似文献
  • 相关主题

摘要

The yeast protein Spa2p localizes to growth sites and is important for polarized morphogenesis during budding, mating, and pseudohyphal growth. To better understand the role of Spa2p in polarized growth, we analyzed regions of the protein important for its function and proteins that interact with Spa2p. Spa2p interacts with Pea2p and Bud6p (Aip3p) as determined by the two-hybrid system; all of these proteins exhibit similar localization patterns, and spa2Δ,pea2Δ, and bud6Δ mutants display similar phenotypes, suggesting that these three proteins are involved in the same biological processes. Coimmunoprecipitation experiments demonstrate that Spa2p and Pea2p are tightly associated with each other in vivo. Velocity sedimentation experiments suggest that a significant portion of Spa2p, Pea2p, and Bud6p cosediment, raising the possibility that these proteins form a large, 12S multiprotein complex. Bud6p has been shown previously to interact with actin, suggesting that the 12S complex functions to regulate the actin cytoskeleton. Deletion analysis revealed that multiple regions of Spa2p are involved in its localization to growth sites. One of the regions involved in Spa2p stability and localization interacts with Pea2p; this region contains a conserved domain, SHD-II. Although a portion of Spa2p is sufficient for localization of itself and Pea2p to growth sites, only the full-length protein is capable of complementing spa2 mutant defects, suggesting that other regions are required for Spa2p function. By using the two-hybrid system, Spa2p and Bud6p were also found to interact with components of two mitogen-activated protein kinase (MAPK) pathways important for polarized cell growth. Spa2p interacts with Ste11p (MAPK kinase [MEK] kinase) and Ste7p (MEK) of the mating signaling pathway as well as with the MEKs Mkk1p and Mkk2p of the Slt2p (Mpk1p) MAPK pathway; for both Mkk1p and Ste7p, the Spa2p-interacting region was mapped to the N-terminal putative regulatory domain. Bud6p interacts with Ste11p. The MEK-interacting region of Spa2p corresponds to the highly conserved SHD-I domain, which is shown to be important for mating and MAPK signaling. spa2 mutants exhibit reduced levels of pheromone signaling and an elevated level of Slt2p kinase activity. We thus propose that Spa2p, Pea2p, and Bud6p function together, perhaps as a complex, to promote polarized morphogenesis through regulation of the actin cytoskeleton and signaling pathways.
机译：酵母蛋白Spa2p定位于生长位点，对于芽，交配和假菌丝生长期间的极化形态发生非常重要。为了更好地理解Spa2p在极化生长中的作用，我们分析了对其功能重要的蛋白质区域以及与Spa2p相互作用的蛋白质。 Spa2p与Pea2p和Bud6p（Aip3p）相互作用，这是由两个杂交系统确定的。所有这些蛋白质都表现出相似的定位模式，并且 spa2 Δ， pea2 Δ和 bud6 Δ突变体表现出相似的表型，表明这三种蛋白质参与相同的生物过程。免疫共沉淀实验表明，Spa2p和Pea2p在体内彼此紧密结合。速度沉降实验表明，Spa2p，Pea2p和Bud6p的显着部分成膜，增加了这些蛋白质形成大型12S多蛋白复合物的可能性。先前已显示Bud6p与肌动蛋白相互作用，这表明12S复合体具有调节肌动蛋白细胞骨架的功能。缺失分析表明，Spa2p的多个区域都参与了其到生长位点的定位。 Spa2p稳定性和本地化涉及的区域之一与Pea2p相互作用。该区域包含一个保守域SHD-II。尽管一部分Spa2p足以将其自身和Pea2p定位于生长位点，但只有全长蛋白能够弥补 spa2 突变缺陷，这表明Spa2p功能还需要其他区域。通过使用双杂交系统，还发现Spa2p和Bud6p与两个对有极化细胞生长重要的促分裂原活化蛋白激酶（MAPK）途径的成分相互作用。 Spa2p与交配信号通路的Ste11p（MAPK激酶[MEK]激酶）和Ste7p（MEK）以及Slt2p（Mpk1p）MAPK通路的MEK Mkk1p和Mkk2p相互作用;对于Mkk1p和Ste7p，Spa2p相互作用区域都映射到N端假定的调节域。 Bud6p与Ste11p进行交互。 Spa2p的MEK相互作用区域对应于高度保守的SHD-1域，这对交配和MAPK信号传导非常重要。 spa2 突变体的信息素信号传导水平降低，而Slt2p激酶活性升高。因此，我们提出Spa2p，Pea2p和Bud6p可能一起发挥功能，通过调节肌动蛋白细胞骨架和信号通路来促进极化形态发生。

著录项

相似文献

  • 外文文献
  • 中文文献
  • 专利
获取原文

客服邮箱：kefu@zhangqiaokeyan.com

京公网安备：11010802029741号 ICP备案号：京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有

  • 客服微信

  • 服务号