Publications by authors named "G Ammerer"
Autophagy is initiated by the assembly of multiple autophagy-related proteins that form the phagophore assembly site where autophagosomes are formed. Atg13 is essential early in this process, and a hub of extensive phosphorylation. How these multiple phosphorylations contribute to autophagy initiation, however, is not well understood.
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- Mineral resource policy is expanding beyond industrial and trade concerns to include environmental protection and social development, creating 'wicked problems' due to conflicting stakeholder opinions.
- The redevelopment of the 'Austrian Mineral Resources Strategy' uses Q-methodology to identify and analyze four different policy framings and their conflicts, particularly between an economy-centric approach and a more integrated policy perspective.
- The findings indicate a preference for economic growth and domestic mineral extraction, suggesting that this narrow focus may overlook important issues like international equity in resource distribution.
In Saccharomyces cerevisiae, impairment of protein phosphatase PP2A leads to temperature and hyperosmotic stress sensitivity, yet the underlying mechanism and the scope of action of the phosphatase in the stress response remain elusive. Using a quantitative mass spectrometry-based approach we have identified a set of putative substrate proteins that show both hyperosmotic stress- and PP2A-dependent changes in their phosphorylation pattern. A comparative analysis with published MS-shotgun data revealed that the phosphorylation status of many of these sites is regulated by the MAPKAP kinase Rck2, suggesting that the phosphatase antagonizes Rck2 signaling.
View Article and Find Full Text PDFThe cell wall integrity (CWI) signaling pathway is best known for its roles in cell wall biogenesis. However, it is also thought to participate in the response to genotoxic stress. The stress-activated protein kinase Mpk1 (Slt2, is activated by DNA damaging agents through an intracellular mechanism that does not involve the activation of upstream components of the CWI pathway.
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- Environmental cues can change cellular behavior traditionally through kinases (activators) and phosphatases (antagonists), but this study highlights a phosphatase-driven mechanism that induces phosphorylation instead.
- Using Saccharomyces cerevisiae, the research shows that the inhibition of a specific phosphatase (PP2A-Cdc55) by Endosulfine triggers a phosphorylation response without the activation of kinases.
- This phosphatase-centric signaling approach challenges the conventional view, suggesting that phosphatases can act as key effectors in cellular responses, influencing various processes vital for surviving stress.