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Becker, T.* ; Cappel, C.* ; Di Matteo, F.* ; Sonsalla, G. ; Kaminska, E.* ; Spada, F.* ; Cappello, S.* ; Damme, M.* ; Kielkowski, P.*

AMPylation profiling during neuronal differentiation reveals extensive variation on lysosomal proteins.

iScience 24:103521 (2021)
Verlagsversion Forschungsdaten DOI PMC
Open Access Gold
Creative Commons Lizenzvertrag
Protein AMPylation is a posttranslational modification with an emerging role in neurodevelopment. In metazoans 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 AMPylation remains largely unknown. Particularly problematic is the localization of thus far identified AMPylated proteins and putative AMP-transferases. We show that protein AMPylation is likely a posttranslational modification of luminal lysosomal proteins characteristic in differentiating neurons. Through a combination of chemical proteomics, gel-based separation of modified and unmodified proteins, and an activity assay, we determine that the modified, lysosomal soluble form of exonuclease PLD3 increases dramatically during neuronal maturation and that AMPylation correlates with its catalytic activity. Together, our findings indicate that AMPylation is a so far unknown lysosomal posttranslational modification connected to neuronal differentiation and it may provide a molecular rationale behind lysosomal storage diseases and neurodegeneration.
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Publikationstyp Artikel: Journalartikel
Dokumenttyp Wissenschaftlicher Artikel
Schlagwörter Cell Biology ; Classification Description ; Molecular Biology ; Neuroscience; Cells; Identification; Expression; Binding; Pld3
Sprache englisch
Veröffentlichungsjahr 2021
HGF-Berichtsjahr 2021
ISSN (print) / ISBN 2589-0042
e-ISSN 2589-0042
Zeitschrift iScience
Quellenangaben Band: 24, Heft: 12, Seiten: , Artikelnummer: 103521 Supplement: ,
Verlag Elsevier
Verlagsort Amsterdam ; Bosten ; London ; New York ; Oxford ; Paris ; Philadelphia ; San Diego ; St. Louis
Begutachtungsstatus Peer reviewed
Institut(e) Institute of Stem Cell Research (ISF)
POF Topic(s) 30204 - Cell Programming and Repair
Forschungsfeld(er) Stem Cell and Neuroscience
PSP-Element(e) G-500800-001
Förderungen Deutsche Forschungsgemeinschaft (DFG, German Research foundation)
LMU excellent Junior Fund
Liebig fellowship from Fund of the association of the chemical industry (VCI)
DOI 10.1016/j.isci.2021.103521
WOS ID WOS:000740252700009
Scopus ID 85120700772
PubMed ID 34917898
Erfassungsdatum 2021-12-22
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