The DOI matches its Crossref record; 62 of the 62 references it cites were found in a registry or an index.
The PQ-loop protein Any1 segregates Drs2 and Neo1 functions required for viability and plasma membrane phospholipid asymmetry
Open accessAbstract
Membrane asymmetry is a key organizational feature of the plasma membrane. Type IV P-type ATPases (P4-ATPases) are phospholipid flippases that establish membrane asymmetry by translocating phospholipids, such as phosphatidylserine (PS) and phospatidylethanolamine, from the exofacial leaflet to the cytosolic leaflet. Saccharomyces cerevisiae expresses five P4-ATPases: Drs2, Neo1, Dnf1, Dnf2, and Dnf3. The inactivation of Neo1 is lethal, suggesting Neo1 mediates an essential function not exerted by the other P4-ATPases. However, the disruption of ANY1 , which encodes a PQ-loop membrane protein, allows the growth of neo1Δ and reveals functional redundancy between Golgi-localized Neo1 and Drs2. Here we show Drs2 PS flippase activity is required to support neo1Δ any1Δ viability. Additionally, a Dnf1 variant with enhanced PS flipping ability can replace Drs2 and Neo1 function in any1Δ cells. any1Δ also suppresses drs2Δ growth defects but not the loss of membrane asymmetry. Any1 overexpression perturbs the growth of cells but does not disrupt membrane asymmetry. Any1 coimmunoprecipitates with Neo1, an association prevented by the Any1-inactivating mutation D84G. These results indicate a critical role for PS flippase activity in Golgi membranes to sustain viability and suggests Any1 regulates Golgi membrane remodeling through protein-protein interactions rather than a previously proposed scramblase activity.
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The yeast ortholog of CG13784 (ANY1) has been found to suppress loss of lipid flippases that act in endosome-to-Golgi recycling.
“the yeast ortholog of CG13784 (ANY1) has been found to suppress loss of lipid flippases that act in endosome-to-Golgi recycling [67,68].”
From Functional unknomics: Systematic screening of conserved genes of unknown function (2023) · cites this paper as [68]
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Metadata
- Authors
- Takar, M., Huang, Y., & Graham, T. R.
- Affiliations
- Vanderbilt University (US)
- Corresponding author
- Graham, Todd R.
- Venue
- Journal of Lipid Research
- Publisher
- Elsevier BV
- Published
- 2019-05
- Volume
- 60
- Issue
- 5
- Pages
- 1032-1042
- ISSN
- 0022-2275 (ISSN-L)
- PMC
- PMC6495175
- OpenAlex
- W2920672763
- Cited by
- 12
- References
- 62
- Citations by year
- 2026: 2 · 2025: 1 · 2023: 2 · 2022: 2 · 2021: 2 · 2020: 2 · 2019: 1
- FWCI
- 0.58
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Lipid Research (publishedVersion, cc-by)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Funders
- National Institutes of Health (GM107978)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Lipid Membrane Structure and Behavior
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Lipid metabolism and biosynthesis
- Keywords
- P4-ATPase, phospholipid flippase, phosphatidylserine, membrane asymmetry, plasma membrane, Golgi membranes, functional redundancy, protein-protein interaction, Saccharomyces cerevisiae
- MeSH terms
- Adenosine Triphosphatases, Calcium-Transporting ATPases, Cell Membrane, Mutation, Phospholipids, Saccharomyces cerevisiae, Membrane Transport Proteins, Saccharomyces cerevisiae Proteins, Phospholipid Transfer Proteins
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