Genome-wide analysis of the response to protein glycosylation deficiency in yeast

Cullen, Paul J.; Xu-Friedman, Rufeng; Delrow, Jeffrey J.; Sprague, G. F.

doi:10.1111/j.1567-1364.2010.00683.x

Cited by 2 publications

(2 citation statements)

References 2 publications

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“…Both, the CWI and the SVG pathways boost inter alia the biosynthesis of cell wall mannoproteins to counteract cell wall defects [121,122]. In addition, the UPR is activated to deal with the high protein load of the ER.…”

Section: Protein O-mannosylation In An Essential Protein Modificationmentioning

confidence: 99%

Protein O-mannosylation: What we have learned from baker's yeast

Loibl

Strahl

2013

Biochimica et Biophysica Acta (BBA) - Molecular Cell Research

108

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Understanding of the molecular mechanisms of protein O-mannosylation in yeast could lead to the development of novel antifungal drugs. In addition, transfer of the knowledge from yeast to mammals could help to develop diagnostic and therapeutic approaches in the frame of neuromuscular diseases. This article is part of a Special Issue entitled: Functional and structural diversity of endoplasmic reticulum.

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Section: Protein O-mannosylation In An Essential Protein Modificationmentioning

confidence: 99%

Protein O-mannosylation: What we have learned from baker's yeast

Loibl

Strahl

2013

Biochimica et Biophysica Acta (BBA) - Molecular Cell Research

108

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“…Previous studies have indicated that protein glycosylation is important for proper MAPK signaling, particularly within the FG pathway. ,− One study reported a high basal level of activation of Kss1 in cells bearing partial loss-of-function alleles of genes needed for O-linked and N-linked glycosylation . Another study reported FUS1-lacZ induction when a specific type of O-glycosylation was absent and when the cells were treated with tunicamycin, a pharmacological inhibitor of protein N-glycosylation.…”

Section: Discussionmentioning

confidence: 99%

Proper Protein Glycosylation Promotes Mitogen-Activated Protein Kinase Signal Fidelity

2012

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The ability of cells to sense and respond appropriately to changing environmental conditions is often mediated by signal transduction pathways that employ mitogen-activated protein kinases (MAPKs). In the yeast Saccharomyces cerevisiae, the high osmolarity glycerol (HOG) and the filamentous growth (FG) pathways are activated following hyperosmotic stress and nutrient deprivation, respectively. Whereas the HOG pathway requires the MAPK Hog1, the FG pathway employs the MAPK Kss1. We conducted a comprehensive screen of nearly 5,000 gene deletion strains for mutants that exhibit inappropriate cross-talk between the HOG and FG pathways. We identified two novel mutants, mnn10Δ and mnn11Δ, that allow activation of Kss1 under conditions that normally stimulate Hog1. MNN10 and MNN11 encode mannosyltransferases that are part of the N-glycosylation machinery within the Golgi apparatus; deletion of either gene results in N-glycosylated proteins that have shorter mannan chains. Deletion of the cell surface mucin Msb2 suppressed the mnn11Δ phenotype, while mutation of a single glycosylation site within Msb2 was sufficient to confer inappropriate activation of Kss1 by salt stress. These findings reveal new components of the N-glycosylation machinery needed to ensure MAPK signaling fidelity.

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Genome-wide analysis of the response to protein glycosylation deficiency in yeast

Cited by 2 publications

References 2 publications

Protein O-mannosylation: What we have learned from baker's yeast

Protein O-mannosylation: What we have learned from baker's yeast

Proper Protein Glycosylation Promotes Mitogen-Activated Protein Kinase Signal Fidelity

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