ArticlePloS one2013
Localization of lipid raft proteins to the plasma membrane is a major function of the phospholipid transfer protein Sec14.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
6 citing papers in PubMed, 14 citations in OpenAlex.
- The interaction networks of small rubber particle proteins in the latex ofFrontiers in plant science · 2024Article
- Kingdom Chromista and its eight phyla: a new synthesis emphasising periplastid protein targeting, cytoskeletal and periplastid evolution, and ancient divergences.Protoplasma · 2018Article
- Article
- Phosphatidylinositol binding of Saccharomyces cerevisiae Pdr16p represents an essential feature of this lipid transfer protein to provide protection against azole antifungals.Biochimica et biophysica acta · 2014Article
- Plasma membrane lipid-protein interactions affect signaling processes in sterol-biosynthesis mutants in Arabidopsis thaliana.Frontiers in plant science · 2014Article
- Modulation of phosphorylation of tocopherol and phosphatidylinositol by hTAP1/SEC14L2-mediated lipid exchange.PloS one · 2014Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The Sec14 protein domain is a conserved tertiary structure that binds hydrophobic ligands. The Sec14 protein from Saccharomyces cerevisiae is essential with studies of S. cerevisiae Sec14 cellular function facilitated by a sole temperature sensitive allele, sec14(ts). The sec14(ts) allele encodes a protein with a point mutation resulting in a single amino acid change, Sec14(G266D). In this study results from a genome-wide genetic screen, and pharmacological data, provide evidence that the Sec14(G266D) protein is present at a reduced level compared to wild type Sec14 due to its being targeted to the proteosome. Increased expression of the sec14(ts) allele ameliorated growth arrest, but did not restore the defects in membrane accumulation or vesicular transport known to be defective in sec14(ts) cells. We determined that trafficking and localization of two well characterized lipid raft resident proteins, Pma1 and Fus-Mid-GFP, were aberrant in sec14(ts) cells. Localization of both lipid raft proteins was restored upon increased expression of the sec14(ts) allele. We suggest that a major function provided by Sec14 is trafficking and localization of lipid raft proteins.
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