ArticleMolecular & cellular proteomics : MCP2017
Study of the Plasma Membrane Proteome Dynamics Reveals Novel Targets of the Nitrogen Regulation in Yeast.
Article in Molecular & cellular proteomics : MCP, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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10 citing papers in PubMed, 19 citations in OpenAlex.
- Physiological and morphological plasticity in response to nitrogen availability of a yeast widely distributed in the open ocean.FEMS microbiology ecology · 2024Article
- Toxicity and assimilation of cellulosic copper nanoparticles require α-arrestins in S. cerevisiae.Metallomics : integrated biometal science · 2023Article
- α-Arrestins and Their Functions: From Yeast to Human Health.International journal of molecular sciences · 2022Review
- The Bul1/2 Alpha-Arrestins Promote Ubiquitylation and Endocytosis of the Can1 Permease upon Cycloheximide-Induced TORC1-Hyperactivation.International journal of molecular sciences · 2021Article
- Longevity Regulation by Proline Oxidation in Yeast.Microorganisms · 2021Article
- The Polymorphic PolyQ Tail Protein of the Mediator Complex, Med15, Regulates the Variable Response to Diverse Stresses.International journal of molecular sciences · 2020Article
- Yeast α-arrestin Art2 is the key regulator of ubiquitylation-dependent endocytosis of plasma membrane vitamin B1 transporters.PLoS biology · 2019Article
- AMPK-Mediated Regulation of Alpha-Arrestins and Protein Trafficking.International journal of molecular sciences · 2019Review
- The yeast arrestin-related protein Bul1 is a novel actor of glucose-induced endocytosis.Molecular biology of the cell · 2018Article
- Conformation-dependent partitioning of yeast nutrient transporters into starvation-protective membrane domains.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
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6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Yeast cells, to be able to grow on a wide variety of nitrogen sources, regulate the set of nitrogen transporters present at their plasma membrane. Such regulation relies on both transcriptional and post-translational events. Although microarray studies have identified most nitrogen-sensitive genes, nitrogen-induced post-translational regulation has only been studied for very few proteins among which the general amino acid permease Gap1. Adding a preferred nitrogen source to proline-grown cells triggers Gap1 endocytosis and vacuolar degradation in an Rsp5-Bul1/2-dependent manner. Here, we used a proteomic approach to follow the dynamics of the plasma membrane proteome after addition of a preferred nitrogen source. We identified new targets of the nitrogen regulation and four transporters of poor nitrogen sources-Put4, Opt2, Dal5, and Ptr2-that rapidly decrease in abundance. Although the kinetics is different for each transporter, we found that three of them-Put4, Dal5, and Ptr2-are endocytosed, like Gap1, in an Rsp5-dependent manner and degraded in the vacuole. Finally, we showed that Gap1 stabilization at the plasma membrane, through deletion of Bul proteins, regulates the abundance of Put4, Dal5 and Ptr2.
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