ArticleThe Journal of cell biology2014
Bem1p contributes to secretory pathway polarization through a direct interaction with Exo70p.
Article in The Journal of cell biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 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.
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.
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Who cites it
19 citing papers in PubMed, 34 citations in OpenAlex.
- Regulation of yeast polarized exocytosis by phosphoinositide lipids.Cellular and molecular life sciences : CMLS · 2024Review
- Exploring the consequences of redirecting an exocytic Rab onto endocytic vesicles.Molecular biology of the cell · 2023Article
- Gradient tracking in mating yeast depends on Bud1 inactivation and actin-independent vesicle delivery.The Journal of cell biology · 2022Article
- Article
- A time-resolved interaction analysis of Bem1 reconstructs the flow of Cdc42 during polar growth.Life science alliance · 2020Article
- GIV/Girdin and Exo70 Collaboratively Regulate the Mammalian Polarized Exocytic Machinery.iScience · 2020Article
- Regulation of Cdc42 for polarized growth in budding yeast.Microbial cell (Graz, Austria) · 2020Review
- Transfer of the Septin Ring to Cytokinetic Remnants in ER Stress Directs Age-Sensitive Cell-Cycle Re-entry.Developmental cell · 2019Article
- Temporal regulation of cell polarity via the interaction of the Ras GTPase Rsr1 and the scaffold protein Bem1.Molecular biology of the cell · 2019Article
- Exocyst dynamics during vesicle tethering and fusion.Nature communications · 2018Article
- A broadly conserved NERD genetically interacts with the exocyst to affect root growth and cell expansion.Journal of experimental botany · 2018Article
- Two subunits of the exocyst, Sec3p and Exo70p, can function exclusively on the plasma membrane.Molecular biology of the cell · 2018Article
- Regulation of Cell Polarity by Exocyst-Mediated Trafficking.Cold Spring Harbor perspectives in biology · 2018Review
- Distinct roles of the polarity factors Boi1 and Boi2 in the control of exocytosis and abscission in budding yeast.Molecular biology of the cell · 2017Article
- Rewiring a Rab regulatory network reveals a possible inhibitory role for the vesicle tether, Uso1.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Analysis of Exocyst Subunit EXO70 Family Reveals Distinct Membrane Polar Domains in Tobacco Pollen Tubes.Plant physiology · 2017Article
- Sec3 promotes the initial binary t-SNARE complex assembly and membrane fusion.Nature communications · 2017Article
- Heterotrimeric G Protein-coupled Receptor Signaling in Yeast Mating Pheromone Response.The Journal of biological chemistry · 2016Review
- Formins: linking cytoskeleton and endomembranes in plant cells.International journal of molecular sciences · 2014Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The exocyst serves to tether secretory vesicles to cortical sites specified by polarity determinants, in preparation for fusion with the plasma membrane. Although most exocyst components are brought to these sites by riding on secretory vesicles as they are actively transported along actin cables, Exo70p displays actin-independent localization to these sites, implying an interaction with a polarity determinant. Here we show that Exo70p directly and specifically binds to the polarity determinant scaffold protein Bem1p. The interaction involves multiple domains of both Exo70p and Bem1p. Mutations in Exo70p that disrupt its interaction with Bem1, without impairing its interactions with other known binding partners, lead to the loss of actin-independent localization. Synthetic genetic interactions confirm the importance of the Exo70p-Bem1p interaction, although there is some possible redundancy with Sec3p and Sec15p, other exocyst components that also interact with polarity determinants. Similar to Sec3p, the actin-independent localization of Exo70p requires a synergistic interaction with the phosphoinositide PI(4,5)P2.
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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.