ArticleMolecular biology of the cell2007
The plasma membrane proteins Prm1 and Fig1 ascertain fidelity of membrane fusion during yeast mating.
Article in Molecular biology of the cell, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
43 citing papers in PubMed, 87 citations in OpenAlex.
- High-Affinity Plasma Membrane CaInternational journal of molecular sciences · 2024Article
- A Velvet Transcription Factor Specifically Activates Mating through a Novel Mating-Responsive Protein in the Human Fungal Pathogen Cryptococcus deneoformans.Microbiology spectrum · 2022Article
- The Sur7 cytoplasmic C terminus regulates morphogenesis and stress responses in Candida albicans.Molecular microbiology · 2021Article
- A zygote-based assay to evaluate intranuclear shuttling inSTAR protocols · 2021Article
- Structural studies of the shortest extended synaptotagmin with only two C2 domains fromiScience · 2021Article
- A fluorescence-based yeast sensor for monitoring acetic acid.Engineering in life sciences · 2021Article
- Cation Transporters ofBiomolecules · 2021Review
- Plasma Membrane Fusion Is Specifically Impacted by the Molecular Structure of Membrane Sterols During Vegetative Development ofGenetics · 2020Article
- The molecular foundations of zygosis.Cellular and molecular life sciences : CMLS · 2020Review
- Article
- Role of Low-Affinity Calcium System Member Fig1 Homologous Proteins in Conidiation and Trap-Formation of Nematode-trapping Fungus Arthrobotrys oligospora.Scientific reports · 2019Article
- The ancient claudin Dni2 facilitates yeast cell fusion by compartmentalizing Dni1 into a membrane subdomain.Cellular and molecular life sciences : CMLS · 2018Article
- The Claudin Family Protein FigA Mediates CaFrontiers in microbiology · 2018Article
- PRM1 and KAR5 function in cell-cell fusion and karyogamy to drive distinct bisexual and unisexual cycles in the Cryptococcus pathogenic species complex.PLoS genetics · 2017Article
- Sexual pheromone modulates the frequency of cytosolic CaMolecular biology of the cell · 2017Article
- Control of plasma membrane lipid homeostasis by the extended synaptotagmins.Nature cell biology · 2016Article
- Extended synaptotagmins are Ca2+-dependent lipid transfer proteins at membrane contact sites.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- High Transmembrane Voltage Raised by Close Contact Initiates Fusion Pore.Frontiers in molecular neuroscience · 2016Article
- Cell biology of yeast zygotes, from genesis to budding.Biochimica et biophysica acta · 2015Review
- Unisexual versus bisexual mating in Cryptococcus neoformans: Consequences and biological impacts.Fungal genetics and biology : FG & B · 2015Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
As for most cell-cell fusion events, the molecular details of membrane fusion during yeast mating are poorly understood. The multipass membrane protein Prm1 is the only known component that acts at the step of bilayer fusion. In its absence, mutant mating pairs lyse or arrest in the mating reaction with tightly apposed plasma membranes. We show that deletion of FIG 1, which controls pheromone-induced Ca(2+) influx, yields similar cell fusion defects. Although extracellular Ca(2+) is not required for efficient cell fusion of wild-type cells, cell fusion in prm1 mutant mating pairs is dramatically reduced when Ca(2+) is removed. This enhanced fusion defect is due to lysis. Time-lapse microscopy reveals that fusion and lysis events initiate with identical kinetics, suggesting that both outcomes result from engagement of the fusion machinery. The yeast synaptotagmin orthologue and Ca(2+) binding protein Tcb3 has a role in reducing lysis of prm1 mutants, which opens the possibility that the observed role of Ca(2+) is to engage a wound repair mechanism. Thus, our results suggest that Prm1 and Fig1 have a role in enhancing membrane fusion and maintaining its fidelity. Their absence results in frequent mating pair lysis, which is counteracted by Ca(2+)-dependent membrane repair.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.