PHOSPHORYLATION OF THE YEAST PLASMA MEMBRANE ATPASE, PMA1

酵母质膜ATP酶 PMA1 的磷酸化

• 批准号: 7420732
• 负责人: AMY Y CHANG
• 金额: $ 0.29万
• 依托单位: UNIVERSITY OF WASHINGTON
• 依托单位国家: 美国
• 财政年份: 2006
• 资助国家: 美国
• 起止时间: 2006-09-20 至 2007-08-31
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/7420732
• 关键词: cell membrane; membrane proteins; mutant; phosphorylation; role; yeasts

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. The yeast plasma membrane ATPase, Pma1, is an essential polytopic membrane protein. It undergoes constitutive phosphorylation on Ser and Thr residues. Pma1 mutants defective in targeting to or stability at the plasma membrane are hypophosphorylated. We would like to identify phosphorylation sites on Pma1 to determine the role of this modification on Pma1 function, targeting, and/or stability.

本子项目是利用由NIH/NCRR资助的中心赠款提供的资源的众多研究子项目之一。子项目和研究者（PI）可能已经从另一个NIH来源获得了主要资金，因此可以在其他CRISP条目中表示。列出的机构是中心的，不一定是研究者的机构。酵母质膜atp酶Pma1是一种重要的多聚膜蛋白。它在丝氨酸和苏氨酸残基上发生本构磷酸化。Pma1突变体在靶向质膜或质膜稳定性方面有缺陷是低磷酸化的。我们希望确定Pma1上的磷酸化位点，以确定这种修饰对Pma1功能、靶向性和/或稳定性的作用。