ArticleProceedings of the National Academy of Sciences of the United States of America2007
Identification of yeast proteins necessary for cell-surface function of a potassium channel.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 54 citations in OpenAlex.
- A high-throughput genetic screening protocol to measure lipid bilayer stress-induced unfolded protein response inSTAR protocols · 2021Article
- Potential Physiological Relevance of ERAD to the Biosynthesis of GPI-Anchored Proteins in Yeast.International journal of molecular sciences · 2021Review
- Proteomic Analysis ofFrontiers in microbiology · 2019Article
- Review
- The endosomal trafficking factors CORVET and ESCRT suppress plasma membrane residence of the renal outer medullary potassium channel (ROMK).The Journal of biological chemistry · 2018Article
- Endoplasmic reticulum-associated degradation of the renal potassium channel, ROMK, leads to type II Bartter syndrome.The Journal of biological chemistry · 2017Article
- Tuning the allosteric regulation of artificial muscarinic and dopaminergic ligand-gated potassium channels by protein engineering of G protein-coupled receptors.Scientific reports · 2017Article
- Trafficking of glycosylphosphatidylinositol anchored proteins from the endoplasmic reticulum to the cell surface.Journal of lipid research · 2016Review
- Biosynthesis of GPI-anchored proteins: special emphasis on GPI lipid remodeling.Journal of lipid research · 2016Review
- Expression of three topologically distinct membrane proteins elicits unique stress response pathways in the yeast Saccharomyces cerevisiae.Physiological genomics · 2015Article
- Cdc1 removes the ethanolamine phosphate of the first mannose of GPI anchors and thereby facilitates the integration of GPI proteins into the yeast cell wall.Molecular biology of the cell · 2014Article
- Review
- ESCRT regulates surface expression of the Kir2.1 potassium channel.Molecular biology of the cell · 2014Article
- Conduits of life's spark: a perspective on ion channel research since the birth of neuron.Neuron · 2013Review
- Review
- Sorting of GPI-anchored proteins into ER exit sites by p24 proteins is dependent on remodeled GPI.The Journal of cell biology · 2011Article
- Saccharomyces cerivisiae as a model system for kidney disease: what can yeast tell us about renal function?American journal of physiology. Renal physiology · 2011Article
- Tamm-Horsfall glycoprotein interacts with renal outer medullary potassium channel ROMK2 and regulates its function.The Journal of biological chemistry · 2011Article
- Article
- Cholesterol and ion channels.Sub-cellular biochemistry · 2010Review
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Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
Abstract
Inwardly rectifying potassium (Kir) channels form gates in the cell membrane that regulate the flow of K(+) ions into and out of the cell, thereby influencing the membrane potential and electrical signaling of many cell types, including neurons and cardiomyocytes. Kir-channel function depends on other cellular proteins that aid in the folding of channel subunits, assembly into tetrameric complexes, trafficking of quality-controlled channels to the plasma membrane, and regulation of channel activity at the cell surface. We used the yeast Saccharomyces cerevisiae as a model system to identify proteins necessary for the functional expression of a mammalian Kir channel at the cell surface. A screen of 376 yeast strains, each lacking one nonessential protein localized to the early secretory pathway, identified seven deletion strains in which functional expression of the Kir channel at the plasma membrane was impaired. Six deletions were of genes with known functions in trafficking and lipid biosynthesis (sur4Delta, csg2Delta, erv14Delta, emp24Delta, erv25Delta, and bst1Delta), and one deletion was of an uncharacterized gene (yil039wDelta). We provide genetic and functional evidence that Yil039wp, a conserved, phosphoesterase domain-containing protein, which we named "trafficking of Emp24p/Erv25p-dependent cargo disrupted 1" (Ted1p), acts together with Emp24p/Erv25p in cargo exit from the endoplasmic reticulum (ER). The seven yeast proteins identified in our screen likely impact Kir-channel functional expression at the level of vesicle budding from the ER and/or the local lipid environment at the plasma membrane.
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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.