Regulation of the Yeast Plasma Membrane (H+) ATPase

;​你知道吗？你知道吗？你知道吗？你知道吗？你知道吗？你知道吗？_D k ?d & d；'() * +, -。/ 0 F Microsoft Word 6.0 Document MSWordDoc6;​摘要：Chang磷酸化/去磷酸化反应在介导细胞对环境信号的应答和调节各种细胞功能中起着重要作用。该基金正在研究磷酸化在酵母中的作用，特别是由PMA1基因编码的质膜（H+），它具有关键的生理作用，对细胞活力至关重要。Pma1（由该基因编码的蛋白质）的活性受到包括葡萄糖代谢在内的环境因素的改变。该研究人员已经表明，Pma1的激活是在培养基中对葡萄糖的反应中发生的，是由发生在质膜上的位点特异性去磷酸化介导的。在其通过分泌途径的转运过程中，Pma1在丝氨酸和苏氨酸残基上被组成性磷酸化。该研究人员将利用酵母2杂交系统和与Pma1共免疫沉淀的蛋白质的肽微测序，确定与Pma1特定结构域相互作用的特定激酶。葡萄糖介导的激活缺陷突变体将用于识别葡萄糖调节的磷酸化位点。这些实验将阐明酵母用于响应环境变化和满足生理需要的信号转导机制。它们还将提供磷酸化在信号转导和调控中的信息。*** ;Oh + 0 $ H + 1 $ H + 1 $ H + 1 $ H + 1 $ H + 1 $ H + 1 $ H + 1 $ H + 1 $ H + 1 $ H + 1 $ H + 1 $ H + 1 $ H + 1 $ H + 1 $ H + 1 $R:模板\ WWUSER \ \正常。DOT摘要：Una Solomon @，LD @,LD @ Microsoft Word 6.0 2.0;;E = E l l l l l l l 1 ~。[摘要]9505980 Chang磷酸化/去磷酸化反应对介导细胞对环境信号的反应和调节各种细胞功能很重要。该基金正在研究磷酸化在酵母中的作用，特别是由PMA1基因编码的质膜（H+），它具有关键的生理作用，对细胞活力至关重要。Pma1（由该基因编码的蛋白质）的活性受到包括葡萄糖代谢在内的环境因素的改变。该研究人员已经表明，Pma1的激活是在培养基中对葡萄糖的反应中发生的，是由发生在质膜上的位点特异性去磷酸化介导的。在其通过分泌途径的转运过程中，Pma1在丝氨酸和苏氨酸残基上被组成性磷酸化。该研究人员将利用酵母2杂交系统和与Pma1共免疫沉淀的蛋白质的肽微测序，确定与Pma1特定结构域相互作用的特定激酶。葡萄糖缺陷突变体介导了wi的激活

; R o o t E n t r y F p`D @ C o m p O b j b W o r d D o c u m e n t O b j e c t P o o l k?_D k?_D 4 @ & ' ( ) * + , - . / 0 F Microsoft Word 6.0 Document MSWordDoc Word.Document.6 ; Abstract 9505980 Chang Phosphorylation/dephosphorylation reactions are important for mediating cell response to environmental signals and regulating various cellular functions. This grant is examining the role of phosphorylation in yeast, specifically the plasma membrane (H+( encoded by the PMA1 gene, which has a critical physiological role and is essential for cell viability. The activity of Pma1 (the protein encoded by this gene), is altered by environmental factors including glucose metabolism. This investigator has shown that Pma1 activation which occurs in response to glucose in the medium, is mediated by site-specific dephosphorylation which occurs at the plasma membrane. During its transit through the secretory path, Pma1 is constitutively phosphorylated on serine and threonine residues. This investigator will identify the specific kinases that interact with specific domains of Pma1, using the yeast 2 hybrid system and peptide microsequencing of proteins that co-immunoprecipitate with Pma1. Mutants defective for glucose mediated a activation will be used to identify the gluc ose regulated phosphorylation sites. %%% These experiments will elucidate the signal transduction mechanisms which are used by yeast to respond to environmental changes and to fulfill physiological needs. They will also provide information on phosphorylation in signal transduction and regulation. *** ; Oh +' 0 $ H l D h S u m m a r y I n f o r m a t i o n ( % R:\WWUSER\TEMPLATE\NORMAL.DOT Abstract Una Solomon Una Solomon @ ,LD @ @ ,LD @ Microsoft Word 6.0 2 ; ; e = e l l l l l l l 1 ~ . T a 2 l l l l l ~ l l l l ~ Abstract 9505980 Chang Phosphorylation/dephosphorylation reactions are important for mediating cell response to environmental signals and regulating various cellular functions. This grant is examining the role of phosphorylation in yeast, specifically the plasma membrane (H+( encoded by the PMA1 gene, which has a critical physiological role and is essential for cell viability. The activity of Pma1 (the protein encoded by this gene), is altered by environmental factors including glucose metabolism. This investigator has shown that Pma1 activation which occurs in response to glucose in the medium, is mediated by site-specific dephosphorylation which occurs at the plasma membrane. During its transit through the secretory path, Pma1 is constitutively phosphorylated on serine and threonine residues. This investigator will identify the specific kinases that interact with specific domains of Pma1, using the yeast 2 hybrid system and peptide microsequencing of proteins that co-immunoprecipitate with Pma1. Mutants defective for glucose mediated a activation wi