ArticleScientific reports2017
Positioning of the SCRAMBLED receptor requires UDP-Glc:sterol glucosyltransferase 80B1 in Arabidopsis roots.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Down-regulation of tomato STEROL GLYCOSYLTRANSFERASE 1 perturbs plant development and facilitates viroid infection.Journal of experimental botany · 2023Article
- Sterol Glucosyltransferases Tailor Polysaccharide Accumulation in Arabidopsis Seed Coat Epidermal Cells.Cells · 2021Article
- Ethylene and hydrogen peroxide regulate formation of a sterol-enriched domain essential for wall labyrinth assembly in transfer cells.Journal of experimental botany · 2019Article
- Why Do Plants Convert Sitosterol to Stigmasterol?Frontiers in plant science · 2019Review
- Inactivation of UDP-Glucose Sterol Glucosyltransferases EnhancesFrontiers in plant science · 2019Article
Corrections and comments
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Authors and funding
7 authors.
Funding
Abstract
The biological function of sterol glucosides (SGs), the most abundant sterol derivatives in higher plants, remains uncertain. In an effort to improve our understanding of these membrane lipids we examined phenotypes exhibited by the roots of Arabidopsis (Arabidopsis thaliana) lines carrying insertions in the UDP-Glc:sterol glucosyltransferase genes, UGT80A2 and UGT80B1. We show that although ugt80A2 mutants exhibit significantly lower levels of total SGs they are morphologically indistinguishable from wild-type plants. In contrast, the roots of ugt80B1 mutants are only deficient in stigmasteryl glucosides but exhibit a significant reduction in root hairs. Sub-cellular investigations reveal that the plasma membrane cell fate regulator, SCRAMBLED (SCM), is mislocalized in ugt80B1 mutants, underscoring the aberrant root epidermal cell patterning. Live imaging of roots indicates that SCM:GFP is localized to the cytoplasm in a non cell type dependent manner instead of the hair (H) cell plasma membrane in these mutants. In addition, we provide evidence for the localization of the UGT80B1 enzyme in the plasma membrane. These data lend further support to the notion that deficiencies in specific SGs are sufficient to disrupt normal cell function and point to a possible role for SGs in cargo transport and/or protein targeting to the plasma membrane.
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