ArticlePloS one2018
Localization and functional characterization of the pathogenesis-related proteins Rbe1p and Rbt4p in Candida albicans.
Article in PloS one, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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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.
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Who cites it
4 citing papers in PubMed.
- The C. elegans LON-1 protein requires its CAP domain for function in regulating body size and BMP signaling.Genetics · 2025Article
- Ustilago maydis PR-1-like protein has evolved two distinct domains for dual virulence activities.Nature communications · 2023Article
- ThemSphere · 2021Article
- Comparative Transcriptomics and RNA-Seq-Based Bulked Segregant Analysis Reveals Genomic Basis UnderlyingFrontiers in microbiology · 2021Article
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Authors and funding
5 authors.
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Abstract
Members of the Cysteine-rich secretory protein, Antigen 5 and Pathogenesis-related 1 (CAP) protein superfamily are important virulence factors in fungi but remain poorly characterized on molecular level. Here, we investigate the cellular localization and molecular function of Rbe1p and Rbt4p, two CAP family members from the human pathogen Candida albicans. We unexpectedly found that Rbe1p localizes to budding sites of yeast cells in a disulfide bond-dependent manner. Furthermore, we show that Rbe1p and Rbt4p bind free cholesterol in vitro and export cholesteryl acetate in vivo. These findings suggest a previously undescribed role for Rbe1p in cell wall-associated processes and a possible connection between the virulence attributes of fungal CAP proteins and sterol binding.
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