ArticleGenetics1999
Characterization of the Wsc1 protein, a putative receptor in the stress response of Saccharomyces cerevisiae.
Article in Genetics, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.
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Who cites it
54 citing papers in PubMed, 135 citations in OpenAlex.
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- Resilience in Resistance: The Role of Cell Wall Integrity in Multidrug-Resistant Candida.Journal of fungi (Basel, Switzerland) · 2025Review
- Histopathological observation andFrontiers in microbiology · 2025Article
- Lessons on fruiting body morphogenesis from genomes and transcriptomes ofStudies in mycology · 2023Article
- A peroxidase-derived ligand that inducesFrontiers in cellular and infection microbiology · 2023Article
- Biodegradation of highly crystallized poly(ethylene terephthalate) through cell surface codisplay of bacterial PETase and hydrophobin.Nature communications · 2022Article
- Structure of the Yeast Cell Wall Integrity Sensor Wsc1 Reveals an Essential Role of Surface-Exposed Aromatic Clusters.Journal of fungi (Basel, Switzerland) · 2022Article
- Regulation of Peroxisome Homeostasis by Post-Translational Modification in the Methylotrophic YeastFrontiers in cell and developmental biology · 2022Review
- Differential Requirement for the Cell Wall Integrity Sensor Wsc1p in Diploids Versus Haploids.Journal of fungi (Basel, Switzerland) · 2021Article
- Inactivating the mannose-ethanolamine phosphotransferase Gpi7 confers caspofungin resistance in the human fungal pathogenCell surface (Amsterdam, Netherlands) · 2021Article
- CWI pathway participated in vegetative growth and pathogenicity through a downstream effector AflRlm1 iniScience · 2021Article
- A Three-Dimensional Model of the Yeast Transmembrane Sensor Wsc1 Obtained by SMA-Based Detergent-Free Purification and Transmission Electron Microscopy.Journal of fungi (Basel, Switzerland) · 2021Article
- Free glycans derived fromThe Journal of biological chemistry · 2019Article
- Identification and Functional Testing of Novel Interacting Protein Partners for the Stress Sensors Wsc1p and Mid2p ofG3 (Bethesda, Md.) · 2019Article
- Modelling and molecular docking studies of the cytoplasmic domain of Wsc-family, full-length Ras2p, and therapeutic antifungal compounds.Computational biology and chemistry · 2019Article
- Monitoring Protein Dynamics in ProteinMolecules (Basel, Switzerland) · 2018Article
- Function and Biosynthesis of Cell Wall α-1,3-Glucan in Fungi.Journal of fungi (Basel, Switzerland) · 2017Review
- Metadata Analysis ofInternational journal of biological sciences · 2017Article
- Up against the wall: is yeast cell wall integrity ensured by mechanosensing in plasma membrane microdomains?Applied and environmental microbiology · 2015Review
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Wsc1p, Wsc2p, Wsc3p, and Wsc4p, members of a novel protein family in the yeast Saccharomyces cerevisiae, are putative sensors or receptors in the stress response. Genetic characterization suggests that the WSC family are upstream regulators of the stress-activated PKC1-MAP kinase cascade and are required for the heat shock response and for maintenance of cell wall integrity. The Wsc proteins share sequence characteristics: at their N terminus they have a cysteine motif and a serine/threonine-rich domain predicted to be extracellular, a hydrophobic domain suggested to be transmembranous, and a variable, highly charged C terminus that may be involved in intracellular signaling. Although a role for the WSC genes in maintenance of cell wall integrity has been firmly established, little is known about the properties of the proteins. As reported here, to study its properties in vivo, we epitope tagged the Wsc1 protein. Wsc1p was found to fractionate with the membrane pellet after high-speed centrifugation. Extraction experiments show that Wsc1p is an integral membrane protein present in two forms: one solubilized by detergent, the other Triton X-100 insoluble. Our results also show that Wsc1p is glycosylated and phosphorylated. To characterize the contribution of different domains to the function of Wsc1p, we generated various deletion constructs. Analysis of the properties and function of the mutant proteins shows that the predicted extracellular serine/threonine-rich domain is required for Wsc1p functionality, as well as its glycosylation. A mutant Wsc1 protein lacking the putative transmembrane domain is not functional and partitions to the soluble fraction. Overexpression of full-length Wsc1p inhibits cell growth, with the N terminus alone being sufficient for this inhibition. This suggests that Wsc1p may function in a complex with at least one other protein important for normal cell growth.
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