| Identification of yeast proteins necessary for cell-surface function of a potassium channel. | |
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MedLine Citation:
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PMID: 17989219 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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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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Authors:
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Friederike A Haass; Martin Jonikas; Peter Walter; Jonathan S Weissman; Yuh-Nung Jan; Lily Y Jan; Maya Schuldiner |
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Publication Detail:
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Type: Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S. Date: 2007-11-07 |
Journal Detail:
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Title: Proceedings of the National Academy of Sciences of the United States of America Volume: 104 ISSN: 1091-6490 ISO Abbreviation: Proc. Natl. Acad. Sci. U.S.A. Publication Date: 2007 Nov |
Date Detail:
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Created Date: 2007-11-16 Completed Date: 2008-01-10 Revised Date: 2009-11-18 |
Medline Journal Info:
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Nlm Unique ID: 7505876 Medline TA: Proc Natl Acad Sci U S A Country: United States |
Other Details:
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Languages: eng Pagination: 18079-84 Citation Subset: IM |
Affiliation:
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Department of Physiology, Neuroscience Graduate Program, and Howard Hughes Medical Institute, University of California, San Francisco, CA 94158, USA. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Cell Membrane
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metabolism Gene Deletion Ion Channel Gating Membrane Potentials Potassium Channels / genetics, metabolism, physiology* Saccharomyces cerevisiae / chemistry*, genetics, physiology |
| Grant Support | |
ID/Acronym/Agency:
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R37MH065334/MH/NIMH NIH HHS |
| Chemical | |
Reg. No./Substance:
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0/Potassium Channels |
| Comments/Corrections | |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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