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PreprintCited by 65Neurogenesis and neuroplasticity mechanismsProtein Kinase Regulation and GTPase SignalingGenetics and Neurodevelopmental Disorders

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FICD activity and AMPylation remodelling modulate human neurogenesis

Open access
Kielkowski, Pavel, Buchsbaum, Isabel Y., Kirsch, Volker C., Bach, Nina C., Drukker, Micha, Cappello, Silvia, Sieber, Stephan A.·2019·Nature Communications
DOI 10.1101/787929PMC PMC6981130

Preprint — published as 10.1038/s41467-019-14235-6 · Paper page

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Abstract

Posttranslational modification (PTM) of proteins represents an important cellular mechanism for controlling diverse functions such as signalling, localisation or protein-protein interactions 1 . AMPylation (also termed adenylylation) has recently been discovered as a prevalent PTM for regulating protein activity 2 . In human cells AMPylation has been exclusively studied with the FICD protein 3–6 . Here we investigate the role of AMPylation in human neurogenesis by introducing a cell-permeable propargyl adenosine pronucleotide probe to infiltrate cellular AMPylation pathways and report distinct modifications in intact cancer cell lines, human-derived stem cells, neural progenitor cells (NPCs), neurons and cerebral organoids (COs) via LC-MS/MS as well as imaging methods. A total of 162 AMP modified proteins were identified. FICD-dependent AMPylation remodelling accelerates differentiation of neural progenitor cells into mature neurons in COs, demonstrating a so far unknown trigger of human neurogenesis.

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Metadata

Authors
Kielkowski, P., Buchsbaum, I. Y., Kirsch, V. C., Bach, N. C., Drukker, M., Cappello, S., & Sieber, S. A.
Affiliations
  • Technical University of Munich (DE)
  • Max Planck Institute of Psychiatry (DE)
  • Helmholtz Munich (DE)
Corresponding author
  • Cappello, Silvia
  • Sieber, Stephan A.
ORCID
Venue
Nature Communications
Publisher
openRxiv
Published
2019-10-01
Volume
11
Issue
1
Pages
517-517
ISSN
2041-1723 (ISSN-L)
DOI
10.1101/787929
PMC
PMC6981130
OpenAlex
W3001174176
Cited by
65
References
1
Citations by year
2026: 8 · 2025: 8 · 2024: 8 · 2023: 3 · 2022: 14 · 2021: 12 · 2020: 12
FWCI
4.04
Type
journal article
Language
en
Open access
Licence
cc-by
Locations
  • Nature Communications (publishedVersion, cc-by)
  • bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion)
  • Europe PMC (PubMed Central) (publishedVersion, cc-by)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • RePEc: Research Papers in Economics (submittedVersion)
  • Leiden Repository (Leiden University) (submittedVersion, cc-by)
  • DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion)
  • DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
  • mediaTUM (Technical University of Munich) (submittedVersion, other-oa)
  • Leiden Repository (Leiden University) (submittedVersion)
  • Site cant be reached (submittedVersion, cc-by)
  • MPG.PuRe (Max Planck Society) (submittedVersion, cc-by)
  • PuSH - Publication Server of Helmholtz Zentrum München (submittedVersion, cc-by)
  • Data Archiving and Networked Services (DANS) (submittedVersion, cc-by)
Funders
H2020 European Research Council (725085)
Topics
  • Life Sciences › Neuroscience › Developmental Neuroscience › Neurogenesis and neuroplasticity mechanisms
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Genetics and Neurodevelopmental Disorders
Keywords
AMPylation, adenylylation, post-translational modification, neural progenitor cells, brain organoids, neuronal differentiation
MeSH terms
Adenosine, Adenosine Monophosphate, Amino Acid Sequence, Cathepsin B, Cell Differentiation, Humans, Membrane Proteins, Neurons, Nucleotidyltransferases, Organoids, Protein Processing, Post-Translational, Down-Regulation, Cell Line, Tumor, Neurogenesis, Neural Stem Cells

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