ArticleMolecules and cells2011
Effect of Saccharomyces cerevisiae ret1-1 mutation on glycosylation and localization of the secretome.
Article in Molecules and cells, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
What it found
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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
2 citing papers in PubMed, 21 citations in OpenAlex.
- Depletion of ε-COP in the COPI Vesicular Coat Reduces Cleistothecium Production in Aspergillus nidulans.Mycobiology · 2015Article
- Effects of mutations in the WD40 domain of α-COP on its interaction with the COPI coatomer in Saccharomyces cerevisiae.Journal of microbiology (Seoul, Korea) · 2012Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
To study the effect of the ret1-1 mutation on the secretome, the glycosylation patterns and locations of the secretory proteins and glycosyltransferases responsible for glycosylation were investigated. Analyses of secretory proteins and cell wall-associated glycoproteins showed severe impairment of glycosylation in this mutant. Results from 2D-polyacrylamide gel electrophoresis (PAGE) indicated defects in the glycosylation and cellular localization of SDS-soluble cell wall proteins. Localization of RFP-tagged glycosyltransferase proteins in ret1-1 indicated an impairment of Golgi-to retrograde transport at a non-permissive temperature. Thus, impaired glycosylation caused by the mislocalization of ER resident proteins appears to be responsible for the alterations in the secretome and the increased sensitivity to ER stress in ret1-1 mutant cells.
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Registered trials
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