PHOSPHORYLATION OF THE YEAST PLASMA MEMBRANE ATPASE, PMA1

该子项目是利用NIH/NCRR资助的中心赠款提供的资源的许多研究子项目之一。子项目和研究者（PI）可能从另一个NIH来源获得主要资金，因此可以在其他CRISP条目中表示。所列机构为中心，不一定是研究者所在机构。酵母质膜ATP酶Pma 1是一种必需的多位膜蛋白。它在Ser和Thr残基上进行组成性磷酸化。Pma 1突变体靶向质膜或在质膜上的稳定性缺陷是低磷酸化的。我们希望鉴定Pma 1上的磷酸化位点，以确定这种修饰对Pma 1功能、靶向和/或稳定性的作用。

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.