ArticleMolecular biology of the cell2010
A novel role of the yeast CaaX protease Ste24 in chitin synthesis.
Article in Molecular biology of the cell, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 32 citations in OpenAlex.
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- Identification of chitin synthase activator in Aspergillus niger and its application in citric acid fermentation.Applied microbiology and biotechnology · 2022Article
- Phosphoramidon inhibits the integral membrane protein zinc metalloprotease ZMPSTE24.Acta crystallographica. Section D, Structural biology · 2018Article
- C-terminus Proteolysis and Palmitoylation Cooperate for Optimal Plasma Membrane Localization of RasA inFrontiers in microbiology · 2018Article
- In Vitro and In Vivo Studies on the Structural Organization of Chs3 from Saccharomyces cerevisiae.International journal of molecular sciences · 2017Article
- High resolution genetic mapping uncovers chitin synthase-1 as the target-site of the structurally diverse mite growth inhibitors clofentezine, hexythiazox and etoxazole in Tetranychus urticae.Insect biochemistry and molecular biology · 2014Article
- Reduction and expansion in microsporidian genome evolution: new insights from comparative genomics.Genome biology and evolution · 2013Article
- Review
- The complex interactions of Chs5p, the ChAPs, and the cargo Chs3p.Molecular biology of the cell · 2012Article
- Genomic and proteomic studies on the effects of the insect growth regulator diflubenzuron in the model beetle species Tribolium castaneum.Insect biochemistry and molecular biology · 2012Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Ste24 is a membrane-integral CaaX metalloprotease residing in the endoplasmic reticulum (ER). In yeast, the only known substrate of Ste24 is the mating factor a precursor. A global screening for protein-protein interactions indicated that Ste24 interacts with chitin synthesis deficient (Chs)3, an enzyme required for chitin synthesis. We confirmed this interaction by yeast two-hybrid analyses and mapped the interacting cytoplasmic domains. Next, we investigated the influence of Ste24 on chitin synthesis. In sterile (ste)24Delta mutants, we observed resistance to calcofluor white (CFW), which was also apparent when the cells expressed a catalytically inactive version of Ste24. In addition, ste24Delta cells showed a decrease in chitin levels and Chs3-green fluorescent protein localized less frequently at the bud neck. Overexpression of STE24 resulted in hypersensitivity to CFW and a slight increase in chitin levels. The CFW phenotype of ste24Delta cells could be rescued by its human and insect orthologues. Although Chs3 binds to Ste24, it seems not to be a substrate for this protease. Instead, our data suggest that Chs3 and Ste24 form a complex in the ER that facilitates protease action on prenylated Chs4, a known activator of Chs3 with a C-terminal CaaX motif, leading to a more efficient localization of Chs3 at the plasma membrane.
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