ArticleMolecular biology of the cell1997
Functional analysis of the interaction between Afr1p and the Cdc12p septin, two proteins involved in pheromone-induced morphogenesis.
Article in Molecular biology of the cell, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 46 citations in OpenAlex.
- Septin organization is regulated by the Gpa1 ubiquitination domain and endocytic machinery during the yeast pheromone response.Molecular biology of the cell · 2025Article
- Beyond division and morphogenesis: Considering the emerging roles of septins in plasma membrane homeostasis and cell wall integrity in human fungal pathogens.PLoS pathogens · 2025Article
- Interplay of septin amphipathic helices in sensing membrane-curvature and filament bundling.Molecular biology of the cell · 2021Article
- RGS proteins and septins cooperate to promote chemotropism by regulating polar cap mobility.Current biology : CB · 2015Article
- Synthetic morphology using alternative inputs.PloS one · 2009Article
- Chemical gradients and chemotropism in yeast.Cold Spring Harbor perspectives in biology · 2009Review
- Regulation of distinct septin rings in a single cell by Elm1p and Gin4p kinases.Molecular biology of the cell · 2009Article
- A novel septin-associated protein, Syp1p, is required for normal cell cycle-dependent septin cytoskeleton dynamics in yeast.Genetics · 2008Article
- Saccharomyces cerevisiae Afr1 protein is a protein phosphatase 1/Glc7-targeting subunit that regulates the septin cytoskeleton during mating.Eukaryotic cell · 2008Article
- Article
- The yeast actin cytoskeleton: from cellular function to biochemical mechanism.Microbiology and molecular biology reviews : MMBR · 2006Review
- Septin function in yeast model systems and pathogenic fungi.Eukaryotic cell · 2005Review
- Cell cycle dynamics and quorum sensing in Candida albicans chlamydospores are distinct from budding and hyphal growth.Eukaryotic cell · 2005Article
- Lipid raft polarization contributes to hyphal growth in Candida albicans.Eukaryotic cell · 2004Article
- A monitor for bud emergence in the yeast morphogenesis checkpoint.Molecular biology of the cell · 2003Article
- Candida albicans septin mutants are defective for invasive growth and virulence.Infection and immunity · 2003Article
- Loss of CDC5 function in Saccharomyces cerevisiae leads to defects in Swe1p regulation and Bfa1p/Bub2p-independent cytokinesis.Genetics · 2003Article
- The Glc7p-interacting protein Bud14p attenuates polarized growth, pheromone response, and filamentous growth in Saccharomyces cerevisiae.Eukaryotic cell · 2002Article
- Hyphal tip-associated localization of Cdc42 is F-actin dependent in Candida albicans.Eukaryotic cell · 2002Article
- Bni5p, a septin-interacting protein, is required for normal septin function and cytokinesis in Saccharomyces cerevisiae.Molecular and cellular biology · 2002Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Saccharomyces cerevisiae mating pheromones induce production of Afr1p, a protein that negatively regulates pheromone receptor signaling and is required for normal formation of the projection of cell growth that becomes the site of cell fusion during conjugation. Afr1p interacts with Cdc12p, which belongs to a family of filament-forming proteins termed septins that have been studied primarily for their role in bud morphogenesis and cytokinesis. The significance of the interaction between Afr1p and Cdc12p was tested in this study by examining the effects of AFR1 mutations that destroy the Cdc12p-binding domain. The results demonstrate that sequences in the C-terminal half of Afr1p are required for interaction with Cdc12p and for proper localization of Afr1p to the base of the mating projection. However, the Cdc12p-binding domain was not required for regulation of receptor signaling or for mating projection formation. This result was surprising because cells carrying a temperature-sensitive cdc12-6 mutation were defective in projection formation, indicating a role for Cdc12p in this process. Although the Cdc12p-binding domain was no essential for Afr1p function, this domain did improve the ability of Afr1p to promote morphogenesis, suggesting that the proper localization of Afr1p is important for its function.
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