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.
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