Recombinant Saccharomyces cerevisiae Plasma membrane ATPase 1 (PMA1), partial

1. Pma1 physically interacts with Exo1. PMID: 28727280
2. These data confirm the important role of Asp739 and Arg811 residues for the biogenesis and function of the enzyme, suggesting their importance for defining H+ transport determinants but ruling out, however, the existence of a strong ionic bond (salt bridge) between these two residues and/or importance of such bridge for structure-function relationships in Pma1 H+-ATPase. PMID: 28320286
3. These results indicate changes in the cell lipid composition. Western blot analysis showed the induction of Pma1 level by IM. RT-PCR revealed an increased PMA1 expression after IM treatment. PMID: 27966483
4. Therefore, H(+) extrusion by Pma1 may be important for Ca(2+) influx through Cch1/Mid1. These results suggest that Pma1 interacts physically with Cch1/Mid1 Ca(2+) channels to enhance their activity via its H(+) -pumping activity PMID: 27935186
5. The results prove that Pma1 residues Ser899 and Ser911/Thr912 are phosphorylated in vivo during glucose activation and that these phosphorylations require the first step of glucose metabolism. PMID: 26019146
6. Results suggest that M5 and M6 loop of Pma1 H+-ATPaseplay play an important role in the protein stability and function. PMID: 24256122
7. M5-M6 loop residues play an important role in protein stability and function, and they are probably responsible for proper arrangement of transmembrane segments M5 and M6 and other domains of enzyme. This might also be important for regulation of enzyme. PMID: 25754037
8. propose a model in which Sod1p maximizes Pma1p activity in two ways: one involving signaling through CK1gamma casein kinases and an independent role for Sod1p in oxidative stress protection PMID: 25956063
9. The results indicate the important role for the Pma1 Asp-714 residue in biogenesis, structure stability, and enzyme function. PMID: 25707108
10. loss of V-ATPase-mediated organelle acidification signals ubiquitination, internalization, and degradation of a portion of Pma1p as a means of balancing overall pH homeostasis PMID: 25271159
11. C-terminus profoundly influences the structure, biogenesis, and function of the yeast H+-ATPase. PMID: 24186948
12. These results indicate that the induction of the two cell transporter genes(Pdr12 and PMA1) plays an important role in acid excretion by the aci mutants of Saccharomyces cerevisiae. PMID: 23667093
13. suppressor mutations disrupt the interaction between the mutant and wild type enzymes, and this enables the wild type Pma1 to reach the plasma membrane PMID: 23825623
14. Negative interaction between PMA1e and MKT1e is mediated by alterations in intracellular pH. PMID: 21856932
15. Point mutations in Pma1 H+-ATPase of Saccharomyces cerevisiae: influence on its expression and activity PMID: 21073429
16. the backbone carbonyl oxygen of Ile-282 contributes directly to proton translocation in PMA1 PMID: 15829483
17. Results suggest that ubiquitylation of Pma1-10 represents a component of a quality control mechanism that targets the misfolded protein for removal from the plasma membrane. PMID: 16410553
18. the Ptk2 carboxyl terminus is essential for glucose-dependent Pma1 activation and for the phosphorylation of Ser899 PMID: 16510118
19. Yeast Pma1 H+-ATPase serves as a model for the role of the C-terminal membrane domain in ATPase stability and targeting to the plasma membrane. PMID: 16751629
20. analysis of degradation pathways for misfolded mutants of the yeast plasma membrane ATPase, Pma1 PMID: 16928681
21. the cooperation of endoplasmic reticulum-associated degradation pathway and the cytoplasm to vacuole targeting pathway is needed for an efficient degradation of misfolded Pma1. PMID: 17238920
22. a mechanism in which the stepwise phosphorylation of two tandemly positioned residues near the C terminus mediates glucose-dependent activation of the H(+)-ATPase. PMID: 17932035
23. Changes in ribosome biogenesis caused by loss of Yvh1 or specific ribosomal proteins have effects on the plasma membrane, perhaps by producing specific translational changes. PMID: 19114459

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KEGG: sce:YGL008C

STRING: 4932.YGL008C