ArticleEukaryotic cell2014
C-terminal truncations of the Saccharomyces cerevisiae PMA1 H+-ATPase have major impacts on protein conformation, trafficking, quality control, and function.
Article in Eukaryotic cell, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 26 citations in OpenAlex.
- Molecular evolution of the members of the Snq2/Pdr18 subfamily of Pdr transporters in the Hemiascomycete yeasts.FEMS yeast research · 2025Article
- Fungal Plasma Membrane HJournal of fungi (Basel, Switzerland) · 2024Review
- Imaging Proteins Sensitive to Direct Fusions Using Transient Peptide-Peptide Interactions.Nano letters · 2023Article
- Enhancing the thermotolerance and erythritol production ofFrontiers in bioengineering and biotechnology · 2023Article
- The plasma membrane HApplied microbiology and biotechnology · 2022Article
- Structure and activation mechanism of the hexameric plasma membrane HNature communications · 2021Article
- A Snf1-related nutrient-responsive kinase antagonizes endocytosis in yeast.PLoS genetics · 2020Article
- Evolutionary and Functional Analysis of aFrontiers in plant science · 2019Article
- Article
- Substrate Insolubility Dictates Hsp104-Dependent Endoplasmic-Reticulum-Associated Degradation.Molecular cell · 2018Article
- A new method for post-translationally labeling proteins in live cells for fluorescence imaging and tracking.Protein engineering, design & selection : PEDS · 2017Article
- Article
- C-terminus of the P4-ATPase ATP8A2 functions in protein folding and regulation of phospholipid flippase activity.Molecular biology of the cell · 2017Article
- Cu/Zn superoxide dismutase and the proton ATPase Pma1p of Saccharomyces cerevisiae.Biochemical and biophysical research communications · 2015Article
- Loss of vacuolar H+-ATPase activity in organelles signals ubiquitination and endocytosis of the yeast plasma membrane proton pump Pma1p.The Journal of biological chemistry · 2014Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The C-terminal tail of yeast plasma membrane (PM) H(+)-ATPase extends approximately 38 amino acids beyond the final membrane-spanning segment (TM10) of the protein and is known to be required for successful trafficking, stability, and regulation of enzyme activity. To carry out a detailed functional survey of the entire length of the tail, we generated 15 stepwise truncation mutants. Eleven of them, lacking up to 30 amino acids from the extreme terminus, were able to support cell growth, even though there were detectable changes in plasma membrane expression, protein stability, and ATPase activity. Three functionally distinct regions of the C terminus could be defined. (i) Truncations upstream of Lys(889), removing more than 30 amino acid residues, yielded no viable mutants, and conditional expression of such constructs supported the conclusion that the stretch from Ala(881) (at the end of TM10) to Gly(888) is required for stable folding and PM targeting. (ii) The stretch between Lys(889) and Lys(916), a region known to be subject to kinase-mediated posttranslational modification, was shown here to be ubiquitinated in carbon-starved cells as part of cellular quality control and to be essential for normal ATPase folding and stability, as well as for autoinhibition of ATPase activity during glucose starvation. (iii) Finally, removal of even one or two residues (Glu(917) and Thr(918)) from the extreme C terminus led to visibly reduced expression of the ATPase at the plasma membrane. Thus, the C terminus is much more than a simple appendage and profoundly influences the structure, biogenesis, and function of the yeast H(+)-ATPase.
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