ArticleMolecular and cellular biology2004
Molecular interactions of yeast Neo1p, an essential member of the Drs2 family of aminophospholipid translocases, and its role in membrane trafficking within the endomembrane system.
Article in Molecular and cellular biology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.
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Who cites it
60 citing papers in PubMed, 117 citations in OpenAlex.
- Recent advances in understanding the regulatory mechanisms of P4-ATPase lipid flippases.Biochemical Society transactions · 2026Review
- Repairing Atp10D in C57Bl/6J mice restores protein expression but does not mitigate metabolic stress from high fat diet.Scientific reports · 2026Article
- Sperm activation for fertilization requires robust activity of the TAT-5 lipid flippase.Developmental biology · 2025Article
- Lipid flippases ATP9A and ATP9B form a complex and contribute to the exocytic pathway from the Golgi.Life science alliance · 2025Article
- Flipping the script: Advances in understanding how and why P4-ATPases flip lipid across membranes.Biochimica et biophysica acta. Molecular cell research · 2024Review
- Arabidopsis flippase ALA3 is required for adjustment of early subcellular trafficking in plant response to osmotic stress.Journal of experimental botany · 2023Article
- Repair of DNA double-strand breaks in plant meiosis: role of eukaryotic RecA recombinases and their modulators.Plant reproduction · 2023Review
- Functional Analysis of the P-Type ATPases Apt2-4 fromJournal of fungi (Basel, Switzerland) · 2023Article
- The phospholipid flippase ATP8B1 is required for lysosomal fusion in macrophages.Cell biochemistry and function · 2022Article
- The lipid flippase Drs2 regulates anterograde transport of Atg9 during autophagy.Autophagy reports · 2022Article
- Toxoplasma gondii phosphatidylserine flippase complex ATP2B-CDC50.4 critically participates in microneme exocytosis.PLoS pathogens · 2022Article
- Structural basis of the P4B ATPase lipid flippase activity.Nature communications · 2021Article
- P-Type ATPase Apt1 of the Fungal PathogenJournal of fungi (Basel, Switzerland) · 2021Article
- Lipid flippases as key players in plant adaptation to their environment.Nature plants · 2021Review
- Dynamic membranes: the multiple roles of P4 and P5 ATPases.Plant physiology · 2021Article
- Lipid flippases in polarized growth.Current genetics · 2021Review
- Arabidopsis Flippases Cooperate with ARF GTPase Exchange Factors to Regulate the Trafficking and Polarity of PIN Auxin Transporters.The Plant cell · 2020Article
- Conserved mechanism of phospholipid substrate recognition by the P4-ATPase Neo1 from Saccharomyces cerevisiae.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2020Article
- A complex genetic interaction implicates that phospholipid asymmetry and phosphate homeostasis regulate Golgi functions.PloS one · 2020Article
- Phospholipid flippases in membrane remodeling and transport carrier biogenesis.Current opinion in cell biology · 2019Review
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Neo1p is an essential yeast member of the highly conserved Drs2 family of P-type ATPases with proposed aminophospholipid translocase activity. Here we present evidence that Neo1p localizes to endosomes and Golgi elements. In agreement with that finding, the temperature-sensitive neo1-37 and neo1-69 mutants exhibit defects in receptor-mediated endocytosis, vacuole biogenesis, and vacuolar protein sorting. Furthermore, neo1 mutants accumulate aberrantly shaped membranous structures most likely derived from vacuoles and the endosomal/Golgi system. At permissive temperatures, HA-Neo1-69p, like wild-type Neo1p, is stable and associates with endosomes. In contrast, HA-Neo1-37p is rapidly degraded and is predominantly retained within the endoplasmic reticulum (ER). Thus, the two neo1 alleles affect the stability and localization of the mutant polypeptides in different ways. A C-terminally truncated and a C-terminally epitope-tagged version of Neo1p are nonfunctional and also mislocalize to the ER. In agreement with a role within the endomembrane system, Neo1p exhibits genetic and physical interactions with Ysl2p, a potential guanine nucleotide exchange factor for Arl1p. Interestingly, deletion of ARL1 rescues the temperature sensitivity of neo1-37 and neo1-69. We demonstrate that Arl1p in its myristoylated and GTP-bound form is responsible for the inhibitory effect. Thus, Neo1p, Ysl2p, and Arl1p represent three proteins that collaborate in membrane trafficking within the endosomal/Golgi system.
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