ArticleThe Journal of biological chemistry2012
Yeast aquaglyceroporins use the transmembrane core to restrict glycerol transport.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 15 citations in OpenAlex.
- Identification ofJournal of fungi (Basel, Switzerland) · 2023Article
- Metabolite secretion in microorganisms: the theory of metabolic overflow put to the test.Metabolomics : Official journal of the Metabolomic Society · 2018Review
- Expression of the aquaglyceroporin HC-9 in a freeze-tolerant amphibian that accumulates glycerol seasonally.Physiological reports · 2017Article
- Central Metabolic Responses to Ozone and Herbivory Affect Photosynthesis and Stomatal Closure.Plant physiology · 2016Article
- Are Aquaporins the Missing Transmembrane Osmosensors?The Journal of membrane biology · 2015Review
- An integrated view on a eukaryotic osmoregulation system.Current genetics · 2015Review
- Expression Analysis of Sugarcane Aquaporin Genes under Water Deficit.Journal of nucleic acids · 2013Article
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Authors and funding
8 authors at 1 institution in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Aquaglyceroporins are transmembrane proteins belonging to the family of aquaporins, which facilitate the passage of specific uncharged solutes across membranes of cells. The yeast aquaglyceroporin Fps1 is important for osmoadaptation by regulating intracellular glycerol levels during changes in external osmolarity. Upon high osmolarity conditions, yeast accumulates glycerol by increased production of the osmolyte and by restricting glycerol efflux through Fps1. The extended cytosolic termini of Fps1 contain short domains that are important for regulating glycerol flux through the channel. Here we show that the transmembrane core of the protein plays an equally important role. The evidence is based on results from an intragenic suppressor mutation screen and domain swapping between the regulated variant of Fps1 from Saccharomyces cerevisiae and the hyperactive Fps1 ortholog from Ashbya gossypii. This suggests a novel mechanism for regulation of glycerol flux in yeast, where the termini alone are not sufficient to restrict Fps1 transport. We propose that glycerol flux through the channel is regulated by interplay between the transmembrane helices and the termini. This mechanism enables yeast cells to fine-tune intracellular glycerol levels at a wide range of extracellular osmolarities.
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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.