ArticleThe EMBO journal2006
Substrate-mediated remodeling of methionine transport by multiple ubiquitin-dependent mechanisms in yeast cells.
Article in The EMBO journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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Who cites it
37 citing papers in PubMed, 72 citations in OpenAlex.
- Glycolysis-dependent sulfur metabolism orchestrates morphological plasticity and virulence in fungi.eLife · 2026Article
- Rethinking the Yeast Endomembrane System.Sub-cellular biochemistry · 2026Review
- Sphingolipid and methionine metabolism in aging.Journal of cell science · 2025Review
- Any1 is a phospholipid scramblase involved in endosome biogenesis.The Journal of cell biology · 2025Article
- A role for Vps13-mediated lipid transfer at the ER-endosome contact site in ESCRT-mediated sorting.The Journal of cell biology · 2024Article
- Recycling of cell surface membrane proteins from yeast endosomes is regulated by ubiquitinated Ist1.The Journal of cell biology · 2022Article
- Exomer complex regulates protein traffic at the TGN through differential interactions with cargos and clathrin adaptor complexes.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2021Article
- Microbial methionine transporters and biotechnological applications.Applied microbiology and biotechnology · 2021Review
- Article
- Elevating PI3P drives select downstream membrane trafficking pathways.Molecular biology of the cell · 2021Article
- Article
- Top-Down Characterization of an Antimicrobial Sanitizer, Leading From Quenchers of Efficacy to Mode of Action.Frontiers in microbiology · 2020Article
- The Siderophore Transporter Sit1 Determines Susceptibility to the Antifungal VL-2397.Antimicrobial agents and chemotherapy · 2019Article
- TORC1 specifically inhibits microautophagy through ESCRT-0.Current genetics · 2019Article
- Article
- Eisosomes are metabolically regulated storage compartments for APC-type nutrient transporters.Molecular biology of the cell · 2018Article
- Budding Yeast Has a Minimal Endomembrane System.Developmental cell · 2018Article
- Distinct complexes of yeast Snx4 family SNX-BARs mediate retrograde trafficking of Snc1 and Atg27.Traffic (Copenhagen, Denmark) · 2017Article
- Identification of the endocytic sorting signal recognized by the Art1-Rsp5 ubiquitin ligase complex.Molecular biology of the cell · 2016Article
- Progress in the microbial production of S-adenosyl-L-methionine.World journal of microbiology & biotechnology · 2016Review
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Plasma membrane transport of single amino-acid methionine in yeast is shown to be mediated by at least seven different permeases whose activities are transcriptionaly and post-transcriptionaly regulated by different ubiquitin-dependent mechanisms. Upon high extracellular methionine exposure, three methionine-permease genes are repressed while four others are induced. SCF(Met30), SCF(Grr1) and Rsp5 ubiquitin ligases are the key actors of the ubiquitin-dependent remodeling of methionine transport. In addition to regulating the activity of Met4, the SCF(Met30) ubiquitin ligase is shown to convey an intracellular signal to a membrane initiated signaling pathway by controlling the nuclear concentration of the Stp1 transcription factor. By coupling intra- and extracellular metabolite sensing, SCF(Met30) thus allows yeast cells to accurately adjust the intermediary sulfur metabolism to the growth conditions. The multiple ubiquitin-dependent mechanisms that function in methionine transport regulation further exemplify the pervasive role of ubiquitin in the adaptation of single-cell organisms to environmental modifications.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.