Matthias Munder

Matthias Munder
Max Planck Institute of Molecular Cell Biology and Genetics | MPI-CBG

About

8
Publications
1,449
Reads
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654
Citations
Additional affiliations
January 2011 - present
February 2010 - September 2010
Martin Luther University Halle-Wittenberg
Position
  • Diploma student
Education
January 2008 - June 2008
October 2004 - October 2010

Publications

Publications (8)
Article
Full-text available
How cells adapt to varying environmental conditions is largely unknown. Here, we show that, in budding yeast, the RNA-binding and stress granule protein Pub1 has an intrinsic property to form condensates upon starvation or heat stress and that condensate formation is associated with cell-cycle arrest. Release from arrest coincides with condensate d...
Article
Full-text available
Cells can enter into a dormant state when faced with unfavorable conditions. However, how cells enter into and recover from this state is still poorly understood. Here, we study dormancy in different eukaryotic organisms and find it to be associated with a significant decrease in the mobility of organelles and foreign tracer particles. We show that...
Article
In search of alternative expression platforms heterologous protein production in microalgae has gained increasing importance in the last years. Particularly, the chloroplast of the green alga Chlamydomonas reinhardtii has been adopted to successfully express foreign proteins like vaccines and antibodies. However, when compared with other expression...
Data
(A) Plasmids used in this study. (B) Antibodies used in this study. (C) Yeast strains used in this study. DOI: http://dx.doi.org/10.7554/eLife.02409.034
Preprint
Full-text available
One of the key questions in biology is how the metabolism of a cell responds to changes in the environment. In budding yeast, starvation causes a drop in intracellular pH, but the functional role of this pH change is not well understood. Here, we show that the enzyme glutamine synthetase (Gln1) forms filaments at low pH and that filament formation...
Article
Several neurodegenerative diseases, such as Parkinson's disease (PD), Alzheimer's disease (AD), Huntington's disease (HD), amyotrophic lateral sclerosis (ALS), or prion diseases, are known for their intimate association with protein misfolding and aggregation. These disorders are characterized by the loss of specific neuronal populations in the bra...
Article
Full-text available
Acute stress causes a rapid redistribution of protein quality control components and aggregation-prone proteins to diverse subcellular compartments. How these remarkable changes come about is not well understood. Using a phenotypic reporter for a synthetic yeast prion, we identified two protein-sorting factors of the Hook family, termed Btn2 and Cu...

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