Abstract
The abundance of yeast plasma membrane H(+)-ATPase on the cell surface is tightly regulated. Modifier of pma1 (mop) mutants were isolated as enhancers of the mutant phenotypes of pma1 mutants. mop2 mutations reduce the abundance and activity of Pma1 protein on the plasma membrane without affecting the abundance of other prominent plasma membrane proteins. The MOP2 gene encodes a 108-kDa protein that has previously been identified both as a gene affecting the yeast cytoskeleton (SLA2) (Holtzman, D.A., Yang, S., and Drubin, D. G. (1993) J. Cell Biol. 122, 635-644) and as a gene affecting endocytosis (END4) (Raths, S., Roher, J., Crausaz, F., and Riezman, H. (1993) J. Cell Biol. 120, 55-65). In some strains, MOP2 (SLA2) is essential for cell viability; in others, a deletion mutant is temperature sensitive for growth. mop2 mutations do not reduce the transcription of PMA1 nor do they lead to the accumulation of Pma1 protein in any intracellular compartment. An epitope-tagged MOP2 protein behaves as a plasma membrane-associated protein whose abundance is proportional to its level of gene expression. Over-expression of MOP2 relieved the toxicity caused by the over-expression of PMA1 from a high copy plasmid; conversely, the growth of mop2 strains was inhibited by the presence of a single extra copy of PMA1. We conclude that MOP2 (SLA2) encodes a plasma membrane-associated protein that is required for the accumulation and/or maintenance of plasma membrane H(+)-ATPase on the cell surface.