Functional and genomic analyses of blocked protein O‐mannosylation in baker's yeast

Arroyo, Javier; Hutzler, Johannes; Bermejo, Clara; Ragni, Enrico; García-Cantalejo, Jesús; Botías, Pedro; Piberger, Heidi; Schott, Andrea; Sanz, Ana B.; Strahl, Sabine

doi:10.1111/j.1365-2958.2011.07537.x

Cited by 59 publications

(62 citation statements)

References 75 publications

(131 reference statements)

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“…OGT1458 was used to analyze genome-wide transcriptional changes in response to inhibition of O-mannosylation. Consistent with the importance of O-mannosylation in wall construction and protein stability, consequences of defective O-mannosylation were activation of the CWI pathway and the unfolded protein response (Arroyo et al 2011). Furthermore, certain genes involved in N-linked mannan outer chain assembly were upregulated.…”

Section: O-mannosylationmentioning

confidence: 60%

“…Furthermore, certain genes involved in N-linked mannan outer chain assembly were upregulated. This, together with the finding that PMT gene transcription is elevated when N-glycosylation is inhibited by tunicamycin (Travers et al 2000), suggests that the N-and O-linked glycans of cell wall mannoproteins can compensate for one another to some extent (Arroyo et al 2011).…”

Section: O-mannosylationmentioning

confidence: 97%

“…The phenotypes of pmt mutants are mimicked by treatment with the rhodanine-3-acetic acid derivative OGT1458, which inhibits PMT activity in vitro (Orchard et al 2004;Arroyo et al 2011). OGT1458 was used to analyze genome-wide transcriptional changes in response to inhibition of O-mannosylation.…”

Section: O-mannosylationmentioning

confidence: 99%

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Architecture and Biosynthesis of the Saccharomyces cerevisiae Cell Wall

2012

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The wall gives a Saccharomyces cerevisiae cell its osmotic integrity; defines cell shape during budding growth, mating, sporulation, and pseudohypha formation; and presents adhesive glycoproteins to other yeast cells. The wall consists of b1,3-and b1,6-glucans, a small amount of chitin, and many different proteins that may bear N-and O-linked glycans and a glycolipid anchor. These components become cross-linked in various ways to form higher-order complexes. Wall composition and degree of cross-linking vary during growth and development and change in response to cell wall stress. This article reviews wall biogenesis in vegetative cells, covering the structure of wall components and how they are cross-linked; the biosynthesis of N-and O-linked glycans, glycosylphosphatidylinositol membrane anchors, b1,3-and b1,6-linked glucans, and chitin; the reactions that cross-link wall components; and the possible functions of enzymatic and nonenzymatic cell wall proteins. TABLE OF CONTENTS Abstract 775Introduction 777

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Section: O-mannosylationmentioning

confidence: 60%

Section: O-mannosylationmentioning

confidence: 97%

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Architecture and Biosynthesis of the Saccharomyces cerevisiae Cell Wall

2012

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“…monosaccharide is extended only by additional mannose residues through the actions of Golgi resident mannosyltransferases of the KTR/MNT and MNN family that use GDP α-D-Man (GDP-Man) as a donor substrate (11). The O-Man glycosylation and the action of multiple PMTs are essential for yeast (14), and O-Man plays major roles in maintaining yeast cell wall integrity (15).…”

mentioning

confidence: 99%

Discovery of a nucleocytoplasmic O-mannose glycoproteome in yeast

Halim

Larsen

Neubert

et al. 2015

Proc. Natl. Acad. Sci. U.S.A.

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Dynamic cycling of N-Acetylglucosamine (GlcNAc) on serine and threonine residues (O-GlcNAcylation) is an essential process in all eukaryotic cells except yeast, including Saccharomyces cerevisiae and Schizosaccharomyces pombe. O-GlcNAcylation modulates signaling and cellular processes in an intricate interplay with protein phosphorylation and serves as a key sensor of nutrients by linking the hexosamine biosynthetic pathway to cellular signaling. A longstanding conundrum has been how yeast survives without O-GlcNAcylation in light of its similar phosphorylation signaling system. We previously developed a sensitive lectin enrichment and mass spectrometry workflow for identification of the human O-linked mannose (O-Man) glycoproteome and used this to identify a pleothora of O-Man glycoproteins in human cell lines including the large family of cadherins and protocadherins. Here, we applied the workflow to yeast with the aim to characterize the yeast O-Man glycoproteome, and in doing so, we discovered hitherto unknown O-Man glycosites on nuclear, cytoplasmic, and mitochondrial proteins in S. cerevisiae and S. pombe.

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“…In eukaryotes, ϳ25-35% of cellular proteins enter the secretory pathway during or after translation by traveling across the endoplasmic reticulum (ER) 4 membrane through protein-conducting channels. During co-translational translocation the translating ribosome is targeted to the ER membrane in a signal recognition particle-dependent manner.…”

mentioning

confidence: 99%

Protein O-Mannosyltransferases Associate with the Translocon to Modify Translocating Polypeptide Chains

Loibl

Wunderle

Hutzler

et al. 2014

Journal of Biological Chemistry

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Background: O-Mannosylation is a conserved, essential protein modification that is initiated in the endoplasmic reticulum (ER). Results: Protein O-mannosyltransferases act at the translocon complex to modify proteins entering the ER. Conclusion: Protein translocation into the ER, O-mannosylation, and N-glycosylation are coordinated processes. Significance: Defining the mechanism of O-mannosylation is crucial to understand its diverse physiological roles for ER homeostasis.

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Functional and genomic analyses of blocked protein O‐mannosylation in baker's yeast

Abstract: Summary O-mannosylation is a crucial protein modification in eukaryotes that is initiated by the essential family of protein O-mannosyltransferases (PMTs). Here we demonstrate that in the model yeast

Cited by 59 publications

References 75 publications

Architecture and Biosynthesis of the Saccharomyces cerevisiae Cell Wall

Architecture and Biosynthesis of the Saccharomyces cerevisiae Cell Wall

Discovery of a nucleocytoplasmic O-mannose glycoproteome in yeast

Protein O-Mannosyltransferases Associate with the Translocon to Modify Translocating Polypeptide Chains

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