ArticleGenetics2009
Conserved WCPL and CX4C domains mediate several mating adhesin interactions in Saccharomyces cerevisiae.
Article in Genetics, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 18 citations in OpenAlex.
- Regulation of the Cell Wall Integrity pathway at the contact site between mating partners in yeast.The Journal of cell biology · 2026Article
- The chitin synthase regulator CSR-3 promotes cellular integrity during cell-cell fusion in the filamentous ascomycete fungus Neurospora crassa.PLoS genetics · 2025Article
- Sticking to the Subject: Multifunctionality in Microbial Adhesins.Journal of fungi (Basel, Switzerland) · 2023Review
- Defining Functions of Mannoproteins inJournal of fungi (Basel, Switzerland) · 2021Article
- Evolutionary Overview of Molecular Interactions and Enzymatic Activities in the Yeast Cell Walls.International journal of molecular sciences · 2020Review
- Adhesins of Yeasts: Protein Structure and Interactions.Journal of fungi (Basel, Switzerland) · 2018Review
- What We Do Not Know about Fungal Cell Adhesion Molecules.Journal of fungi (Basel, Switzerland) · 2018Review
- Molecular mechanism of flocculation self-recognition in yeast and its role in mating and survival.mBio · 2015Article
- Malachite green mediates homodimerization of antibody VL domains to form a fluorescent ternary complex with singular symmetric interfaces.Journal of molecular biology · 2013Article
- Accelerated and adaptive evolution of yeast sexual adhesins.Molecular biology and evolution · 2011Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 2 countries.
Funding
Abstract
Several adhesins are induced by pheromones during mating in Saccharomyces cerevisiae, including Aga1p, Aga2p, Sag1p (Agalpha1p), and Fig2p. These four proteins all participate in or influence a well-studied agglutinin interaction mediated by Aga1p-Aga2p complexes and Sag1p; however, they also play redundant and essential roles in mating via an unknown mechanism. Aga1p and Fig2p both contain repeated, conserved WCPL and CX(4)C domains. This study was directed toward understanding the mechanism underlying the collective requirement of agglutinins and Fig2p for mating. Apart from the well-known agglutinin interaction between Aga2p and Sag1p, three more pairs of interactions in cells of opposite mating type were revealed by this study, including bilateral heterotypic interactions between Aga1p and Fig2p and a homotypic interaction between Fig2p and Fig2p. These four pairs of adhesin interactions are collectively required for maximum mating efficiency and normal zygote morphogenesis. GPI-less, epitope-tagged forms of Aga1p and Fig2p can be co-immunoprecipitated from the culture medium of mating cells in a manner dependent on the WCPL and CX(4)C domains in the R1 repeat of Aga1p. Using site-directed mutagenesis, the conserved residues in Aga1p that interact with Fig2p were identified. Aga1p is involved in two distinct adhesive functions that are independent of each other, which raises the possibility for combinatorial interactions of this protein with its different adhesion receptors, Sag1 and Fig2p, a property of many higher eukaryotic adhesins.
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Registered trials
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