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Giovanna Sonsalla
Researcher at Ludwig Maximilian University of Munich
Publications - 2
Citations - 32
Giovanna Sonsalla is an academic researcher from Ludwig Maximilian University of Munich. The author has contributed to research in topics: Proteome & Adenylylation. The author has an hindex of 1, co-authored 2 publications receiving 12 citations.
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Journal ArticleDOI
CRISPR-Mediated Induction of Neuron-Enriched Mitochondrial Proteins Boosts Direct Glia-to-Neuron Conversion.
Gianluca Luigi Russo,Giovanna Sonsalla,Poornemaa Natarajan,Christopher T. Breunig,Giorgia Bulli,Juliane Merl-Pham,Sabine Schmitt,Jessica Giehrl-Schwab,Florian Giesert,Martin Jastroch,Hans Zischka,Wolfgang Wurst,Stefan H. Stricker,Stefanie M. Hauck,Giacomo Masserdotti,Magdalena Götz +15 more
TL;DR: The comprehensive mitochondrial proteome of cortical astrocytes and neurons is determined, identifying about 150 significantly enriched mitochondrial proteins for each cell type, including transporters, metabolic enzymes, and cell-type-specific antioxidants.
Posted ContentDOI
AMPylation is a specific lysosomal protein posttranslational modification in neuronal maturation
Thomas Becker,Cedric Cappel,Francesco Di Matteo,Giovanna Sonsalla,Ewelina Kaminska,Fabio Spada,Silvia Cappello,Markus Damme,Pavel Kielkowski +8 more
Abstract: Summary Protein AMPylation is a pervasive posttranslational modification with an emerging role in neurodevelopment. In metazoans the two highly conserved protein AMP-transferases together with a diverse group of AMPylated proteins have been identified using chemical proteomics and biochemical techniques. However, the function of this modification remains largely unknown. Particularly problematic is the localization of thus far identified AMPylated proteins and putative AMP-transferases. Here, we uncover protein AMPylation as a novel posttranslational modification of luminal lysosomal proteins characteristic in differentiating neurons. Through a combination of chemical proteomics, advanced gel-based separation of modified and unmodified proteins and activity assay, we show that an AMPylated, lysosomal soluble form of exonuclease PLD3 increases dramatically during neuronal maturation and that AMPylation inhibits its catalytic activity. Together, our findings unveil so far unknown lysosomal posttranslational modification, its connection to neuronal differentiation and putatively provide a novel molecular rationale to design of therapeutics for lysosomal storage diseases.