A Pronucleotide Probe for Live‐Cell Imaging of Protein AMPylation

Kielkowski, Pavel; Buchsbaum, Isabel Y.; Becker, Tobias; Bach, Kathrin; Cappello, Silvia; Sieber, Stephan A.

doi:10.1002/cbic.201900716

Cited by 20 publications

(39 citation statements)

References 26 publications

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“…Sieber, who was featured in this section when he won the Klung‐Wilhelmy Science Prize, disclosed in a Communication in Angewandte Chemie that the cytotoxic natural product vioprolide A targets nucleolar protein 14 . He is on the Editorial Advisory Board of ChemBioChem , where he published a Communication on a pronucleotide probe for live‐cell imaging of protein AMPylation …”

Section: Awarded …mentioning

confidence: 99%

GDCh and DBG Awards 2020

2020

Angew Chem Int Ed

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Each year,t he German Chemical Society (Gesellschaft Deutscher Chemiker,GDCh) and its various divisions recognize outstanding achievements with multifarious prizes.Some of the 2020 awardees who have been regular authors of Angewandte Chemie and its sister journals are featured below. Stefanie Dehnen (University of Marburg, Germany) [1a] is the winner of the Alfred Stock Memorial Award for scientific excellence in inorganic chemistry.Dehnen studied Chemistry at University of Karlsruhe (now Karlsruhe Institute of Te chnology,K IT) and earned her doctoral degree in 1996 for work supervised by Dieter Fenske.She stayed in Karlsruhe,did postdoctoral research in Theoretical Chemistry with Reinhard Ahlrichs (1997), and received her Habilitation in Inorganic Chemistry in 2004. In 2005 she became Professor of Inorganic Chemistry at Philipps University Marburg. Dehnensr esearch is focused on the synthesis and experimental as well as quantum chemical investigation of compounds with multinary,inparticular multimetallic,m olecular nanoarchitectures that have potential as innovative catalysts,w hite-light emitters,o rb attery materials.S he had aC ommunication in Angewandte Chemie on controlling the white-light generation of tin-chalcogene clusters [1b] and aG uest Editorial in favor of original fundamental research. [1c] Dehnen was elected Member of the Board of GDCh in 2019. She is currently Vice President of the GDCh. Markus Antonietti (Max Planck Institute (MPI) for Colloids and Interfaces,P otsdam;G ermany) is presented with the 2020 Hermann Staudinger Award for excellence in macromolecular chemistry.A ntonietti studied at University of Mainz and earned his doctorate under supervision of Hans Sillescu in 1985. He stayed in Mainz for his Habilitation (finished in 1990) and, in 1991, took up ap rofessorship at Philipps University of Marburg. In 1993 he movedt ot he MPIf or Colloids and Interfaces whereh ew as appointedD irectorf or ColloidC hemistry.H ei sa lsoaProfessora tt he University of Potsdam. Antoniettiscurrent research dealsw ithm acromoleculars ystems in sustainable chemistry, i.e. ,f or catalysis ande lectrocatalysis, for artificial photosynthesis,a nd forc arbons equestration ands oilr emediation.I naCommunicationi n Angewandte Chemie,h er eportedo ns ynthetic humica cids that solubilize phosphates to improve soil fertility, [2a] andinChemCatChems"Building A NewE nergyE conomy"S pecial Issueh er eviewed ionicc arbonn itrides in solarh ydrogenp roduction ando rganic synthesis. [2b] Antonietti is am embero f theE ditorial Boardo fSmall ando ft he Executive BoardofW iley-VCHsM acromolecularJ ournals.

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Section: Awarded …mentioning

confidence: 99%

GDCh and DBG Awards 2020

2020

Angew Chem Int Ed

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“…Sieber, der in dieser Rubrik bereits als Gewinner des Klung‐Wilhelmy‐Wissenschaftspreises vertreten war, konnte in einer Angewandte‐Chemie ‐Zuschrift zeigen, dass der zytotoxische Naturstoff Vioprolid A mit dem für die Ribosomen‐Biogenese essentiellen nukleolären Protein 14 interagiert . Er ist Mitglied des Redaktionsbeirat von ChemBioChem ; in dieser Zeitschrift stellte er kürzlich eine Pronucleotid‐Sonde für die Bildgebung der Protein‐AMPylierung in lebenden Zellen vor …”

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Preise der GDCh und DBG 2020

2020

Angewandte Chemie

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“…In contrast, there are only scare data about the SELO's function and protein substrates (Sreelatha et al, 2018). Several complementary strategies were introduced to analyze protein AMPylation, including isotopically labeled adenosine probes (Pieles et al, 2014), radioactively labelled adenosine nucleotides, antibodies (Kingdon et al, 1967;Yarbrough et al, 2009), microarrays (Yu and LaBaer, 2015), N 6 -biotin modified ATP (Sreelatha et al, 2018), and N 6 -propargyl adenosine 5'-O-triphosphate (N6pATP) or phosphoramidate (Broncel et al, 2012;Grammel et al, 2011;Kielkowski et al, 2020bKielkowski et al, , 2020a. We have recently developed a chemical proteomic approach, which allows high-throughput screening of protein AMPylation and comparison of the AMPylation levels between different conditions.…”

Section: Introductionmentioning

confidence: 99%

“…We have recently developed a chemical proteomic approach, which allows high-throughput screening of protein AMPylation and comparison of the AMPylation levels between different conditions. This strategy utilizes the N 6 -propargyl or N 6ethylazide adenosine phosphoramidate (pro-N6pA and pro-N6azA, respectively) probes which upon uptake into cells are metabolically activated to the corresponding N 6 -modified adenosine triphosphate and used by endogenous AMP-transferases for protein AMPylation ( Figure 1B) (Kielkowski et al, 2020b(Kielkowski et al, , 2020a. Of note, the resulting N 6 -modified ATP is inherently in competition with endogenous ATP and thus cannot report on the exact stoichiometry of protein AMPylation.…”

Section: Introductionmentioning

confidence: 99%

AMPylation is a specific lysosomal protein posttranslational modification in neuronal maturation

Becker

Cappel

et al. 2021

Preprint

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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.

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A Pronucleotide Probe for Live‐Cell Imaging of Protein AMPylation

Cited by 20 publications

References 26 publications

GDCh and DBG Awards 2020

GDCh and DBG Awards 2020

Preise der GDCh und DBG 2020

AMPylation is a specific lysosomal protein posttranslational modification in neuronal maturation

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