Functional analysis of the interaction between Afr1p and the Cdc12p septin, two proteins involved in pheromone-induced morphogenesis
Functional analysis of the interaction between Afr1p and the Cdc12p septin, two proteins involved in pheromone-induced morphogenesis
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DOI：
10.1091/mbc.8.6.987
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发表时间：
1997-06-01
影响因子：
3.3
通讯作者：
Konopka, JB
中科院分区：
文献类型：
--
作者：
Giot, L;Konopka, JB
酿酒酵母交配信息素诱导产生Afr 1 p，这是一种负调节信息素受体信号传导的蛋白质，并且是正常形成细胞生长投影所必需的，该投影在接合期间成为细胞融合的位点。Afr 1 p与Cdc 12 p相互作用，Cdc 12 p属于一个被称为septins的蛋白质形成家族，主要研究其在芽形态发生和胞质分裂中的作用。Ahr 1 p和Cdc 12 p之间的相互作用的意义进行了测试，在这项研究中，通过检查AFR 1突变破坏Cdc 12 p结合结构域的影响。结果表明，在C-末端一半的Afr 1 p的序列需要与Cdc 12 p的相互作用和适当的本地化的Afr 1 p的交配投影的基础。然而，Cdc 12 p结合结构域不需要调节受体信号传导或交配投射形成。这一结果令人惊讶，因为携带温度敏感性cdc 12 -6突变的细胞在突起形成中有缺陷，表明Cdc 12 p在此过程中的作用。虽然Cdc 12 p结合结构域不是Afr 1 p功能所必需的，但该结构域确实提高了Afr 1 p促进形态发生的能力，这表明Afr 1 p的适当定位对其功能很重要。
Saccharomyces cerevisiae mating pheromones induce production of Afr1p, a protein that negatively regulates pheromone receptor signaling and is required for normal formation of the projection of cell growth that becomes the site of cell fusion during conjugation. Afr1p interacts with Cdc12p, which belongs to a family of filament-forming proteins termed septins that have been studied primarily for their role in bud morphogenesis and cytokinesis. The significance of the interaction between Ahr1p and Cdc12p was tested in this study by examining the effects of AFR1 mutations that destroy the Cdc12p-binding domain. The results demonstrate that sequences in the C-terminal half of Afr1p are required for interaction with Cdc12p and for proper localization of Afr1p to the base of the mating projection. However, the Cdc12p-binding domain was not required for regulation of receptor signaling or for mating projection formation. This result was surprising because cells carrying a temperature-sensitive cdc12-6 mutation were defective in projection formation, indicating a role for Cdc12p in this process. Although the Cdc12p-binding domain was not essential for Afr1p function, this domain did improve the ability of Afr1p to promote morphogenesis, suggesting that the proper localization of Afr1p is important for its function.